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1. Cell Organells ....................................................... 1 2. Cell Membranes: Structure and Function ....... 3 3. Amino Acids: Structure and Properties ........... 8 4. Proteins: Structure and Function .................... 17 5. Enzymology-I ..................................................... 27 6. Enzymology-II: Iso-Enzymes and Clinical Enzymology ......................................... 40 7. Methods of Separation & Purification of Biological Compounds, Methods of Study of Metabolism ......................................... 47 8. Carbohydrates-I:Chemistry, Digestion and Absorption .......................................................... 52 9. Carbohydrates-II: Major Metabolic Pathways of Glucose, Glycolysis, Gluconeogenesis, Glycogen Metabolism ...... 61 10. Carbohydrates-III: Regulation of Blood Sugar, Insulin and Diabets Mellitus .............. 70 11. Carbohydrates-IV: Other Metabolic Pathways (HMP Shunt Pathway, Fructose, Galactose, Glucuronic Acid, Alcohol) ................................ 81
2 Viva—based on Textbook of Biochemistry 12. Lipids-I: Chemistry, Digestion and Absorption of Lipids ......................................... 88 13. Lipids-II: Metabolism of Fatty acids, Fatty acid oxidation, Fatty acid synthesis, Lipolysis, Ketone bodies ..................................................... 95 14. Lipids-III: Cholesterol, Lipoproteins and Cardiovascular Diseases ................................. 103 15. Lipids-IV: MCFA, PUFA and Prostaglandins .................................................. 112 16. Lipids-V: Compound Lipids ......................... 118 17. Amino Acid Metabolism-I: General: Digestion, Absorption, Transamination, Urea ...................................... 122 18. Amino Acid Metabolism-II: Simple, Hydroxy and Sulfur Containing Amino Acids Glycine, Serine, Alanine, Threonine, Methionine, Cysteine ...................................... 128 19. Amino Acid Metabolism-III: Acidic, Basic and Branched Chain Amino Acids, Glutamic acid, Glutamine, Aspartic acid, Asparagine, Lysine, Nitric Oxide, Valine, Leucine, Isoleucine .... 132 20. Amino Acid Metabolism-IV: Aromatic Amino Acids: Phenyl alanine, Tyrosine, Tryptophan, Histidine ............................................................ 137 21. Amino Acid Metabolism-V: Inter-relations of Amino Acid Metabolisms, One Carbon Metabolism, Amino Acidurias ...................... 142
22. Citric Acid Cycle .............................................. 144 23. Electron Transport Chain ............................... 147 24. Free Radicals and Anti-oxidants ................... 151 25. Plasma Proteins ................................................ 153 26. Immunochemistry ............................................ 156 27. Specialised Proteins: Collagen, Myosin ...... 158 28. Heme Synthesis and Breakdown ................. 160 29. Haemoglobins .................................................. 165 30. Vitamin-I: Fat Soluble Vitamins: A, D, E and K .................................................................. 169 31. Vitamin-II: Water soluble vitamins .............. 174 32. Mineral Metabolism ........................................ 189 33. Energy Metabolism and Nutrition ............... 195 34. Detoxification and Biotransformation of Xenobiotics ........................................................ 199 35. Biochemical Aspects of Environmental Pollution ............................................................ 201 36. Acid Base Balance and pH ............................. 203 37. Electrolyte and Water Balance ....................... 207 38. Molecular Biology-I: Nucleotides, Chemistry and Metabolism ............................................... 209
4 Viva—based on Textbook of Biochemistry 39. Molecular Biology-II: DNA structure and Replication ........................................................ 216 40. Molecular Biology-III: Transcription and Translation ........................................................ 220 41. Molecular Biology-IV: Molecular Genetics and Control of Gene Expression ................... 227 42. Molecular Biology-V: Recombinant DNA Technology and Gene Therapy .................... 229 43. Biochemistry of AIDS ..................................... 233 44. Biochemistry of Cancer ................................... 235 45. Applications of Radio-isotopes in Medicine ............................................................ 238 46. Body Fluids ....................................................... 240 47. Hormones-I: Mechanism of Action of Hormones .......................................................... 242 48. Hormones-II: Pituitary Hormones ................ 244 49. Hormones-III: Steroid Hormones ................. 246 50. Hormones-IV: Thyroid Hormones ............... 248 51. Clinical Biochemistry-I: .................................. 250 52. Clinical Biochemistry-II: Liver and Gastric Function Tests ..................................... 252 53. Clinical Biochemistry-III: Kidney Function Tests .................................................................... 256
Q. What is the function of Golgi complex? A. Maturation and processing of nascent proteins, glycosylation of proteins, secretion newly synthesised proteins (Page 3). Q. What is the function of endoplasmic reticulum? (Page 3) A. Biosynthesis of proteins, drug metabolism, desaturation of fatty acids. Q. What is the marker enzyme for endoplasmic reticulum? A. Glucose-6-phosphatase (Page 3, Table 1.3). Q. Where does protein synthesis take place? A. On the walls of endoplasmic reticulum and also in cytosol (Page 3). Q. What are cathepsins? A. They are intracellular proteolytic enzymes (Page 4).
What is lysozyme? A. Glycolysis (Embden-Meyerhof pathway). HMP shunt pathway.2 Viva—based on Textbook of Biochemistry Q. What is the function of mitochondria? A. Q. Q. necessary for destroying the unwanted free radicals. Fatty acid synthesis. They contain peroxidase and catalase. What are the important metabolic events taking place in mitochondria? A.4). Generation of ATP (See page 5). (Page 4) Q. What are the important metabolic events taking place in cytoplasm? A. What are peroxisomes? A. beta oxidation of fatty acids and urea cycle (Page 5). Table 1. glycogen metabolism. Q. It is an enzyme present in external secretions (Page 35). Synthesis of nucleotides. Degradation of amino acids (See Page 5. . electron transport chain. What is the function of lysosomes? A. Q. TCA cycle. They are bags of hydrolytic enzymes that bring about degradation of macromolecules (Page 4).
How do you describe the structure of cell membrane? A. Q. Q. Phospholipids are arranged in bilayers with a hydrophobic core (Page 6). Membrane is composed of lipid bilayer. Structure and Function 3 Cell Membranes: Structure and Function Q. A. Q. They are enzymes seen on the outer part of cell membrane (Page 6). A. Alkaline phosphatase. Give examples of ecto-enzymes. . but flip-flop movement is restricted (Page 6). 5’nucleotidase (Page 6). Q. The lipid bilayer shows free lateral movement of its components. What are the characteristics of fluid mosaic model?. What are ecto-enzymes? A. What do you mean by fluidity of the membrane? A. Fluid mosaic model (Page 6).Cell Membranes.
Cholesterol and unsaturated fatty acids (Page 6). Q.g. What are the salient features of active transport? A. It is carrier mediated. Ion channels specific for calcium. Q. What are the different types of transport mechanisms? A. They are special devices for quick transport of electrolytes (Page 9). It does not require energy directly (Page 8). Q. Can you give an example of facilitated transport? A. gramicidin (Page 10). valinomycin. What are the salient features of facilitated diffusion? A. Q. What are ion channels? A. Passive and active. e. What are the components of membrane that alter the fluidity? A. Q. Q. potassium and chloride (Page 9). It requires energy. Glucose transporters (Page 8). It requires transporters. They are transport antibiotics which increase the permeability of membrane to ions. A. Transport is generally unidirectional (Page 10). Give some examples of ion channels. Q. .4 Viva—based on Textbook of Biochemistry Q. Passive type is subclassified as simple diffusion and facilitated diffusion (Page 8). What are ionophores? A.
Give examples of uniport. Q. What is its clinical significance? A. Hydrolysis of one molecule of ATP can result in expulsion of 3 sodium ions and influx of 2 potassium ions (Page 10). Q. What is co-transport? A. A. Digoxin increases the contractility of the cardiac muscle. this is maintained by sodium pump. Q. it is called co-transport system (Page 10). It is called sodium-potassium activated ATPase. Q. Give examples of active transport systems. by inhibiting the sodium pump (Page 10). . What is a uniport? A. calcium pump (Page 10).Cell Membranes. Glucose transporter (GluT2) operating in most of the cells is an example. About 40% of the total energy expenditure in a cell is used for this active transport system (Page 10). Calcium pump is another example (Page 10). If transfer of one molecule depends on simultaneous or sequential transfer of another molecule. It carries single solute across the membrane (Page 10). A. Cell has low intracellular sodium. Structure and Function 5 Q. Q. but concentration of potassium inside the cell is high. What is the importance of sodium pump? A. Q. Sodium pump. How does sodium pump work? A.
What is endocytosis?.2. What is antiport system?. Q. Phlorhizin. Sodium dependent glucose transporter (SgluT) (Fig. (Page 10) A.31). In symport.6 Viva—based on Textbook of Biochemistry Q. The antiport system carries two solutes or ions in opposite direction. Q. Q. Low Density Lipoprotein (LDL) binds to the LDL receptor and the complex is later internalised. What is pinocytosis?. Give examples of antiport. Sodium pump (Fig. It is the mechanism by which cells internalise extracellular macromolecules. (Page 11) A.4). The cotransport system may be symport or antiport (Page 10). What is symport? A. an inhibitor of sodium-dependent cotransport of glucose. especially in the proximal convoluted tubules of kidney. Q. . the transporter carries two solutes in the same direction across the membrane (Page 10). (Page 10) A. It is receptor mediated. Q. produces renal damage and results in renal diabetes. Q.7) or chloride-bicarbonate exchange in RBC (Fig. (Page 10) A.8. (Page 11) A. These vesicles are coated with Clathrin. Amino acid transport is another example for symport. . How are co-transport systems classified? A. Give examples of symport.29.
What is phagocytosis. (Page 11) A. .Cell Membranes. During phagocytosis. (Page 11) A. Structure and Function 7 Q. What is respiratory burst. Q. It is the engulfment and internalisation of large particles such as bacteria by macrophages and granulocytes. there is an increase in oxygen consumption with formation of the superoxide ion.
How do you classify amino acids? (Page 12) A. Q. What are hydroxy amino acids? A. Q. Q. Based on the structure. Sulfur containing amino acids.8 Viva—based on Textbook of Biochemistry Amino Acids: Structure and Properties Q. What are branched chain amino acids?(Page 12) A. (Page 12) A. Cysteine and methionine. Name the Sulfur containing amino acids. Valine. Serine and threonine. amino acids are classified into: Simple amino acids. Imino acid and Derived amino acids. A. Acidic amino acids. Heterocyclic amino acids. (Page 12) . Name the acidic amino acids. (Page 12) Q. Basic amino acids. Aspartic acid and glutamic acid. Hydroxy amino acids. Aromatic amino acids. Amino acids with amide group. leucine and isoleucine. Branched chain amino acids.
Give examples of amino acids with hydrophobic side chains. leucine. Arginine and lysine. What are the basic amino acids? A. Guanidinium group (-NH-CNH-NH2). Q. Q. Valine. Methionine. ornithine. Arginine contains which special group? (Page 12) A. Amino acid containing a thio-ether bond is. Give examples of derived amino acids. A. (Page 12) A. Q. citrulline. Hydroxy proline. Lysine and arginine. Which amino acid has a net positive charge at physiological pH? (Page 12) A. Phenylalanine and tyrosine. hydroxy lysine. Q.(Page 12) A. Tryptophan and histidine.Amino Acids: Structure and Properties 9 Q. Give an example of an imino acid. (Page 12) A. (Page 12) Q. Q. homocysteine. isoleucine. (Page 12) (Page 12) Q. Proline. What are heterocyclic amino acids? A. Give the names of aromatic amino acids. Q. Benzene group is present in which amino acid? (Page 12) A. . (Page 12) A. Q. Phenyl alanine.
Proline. Q. Name some hydrophobic amino acids.(Page 12) Q. Q. Tryptophan contains what special group? (Page 12) A. Name some glucogenic amino acids. Ketogenic amino acids enter into the metabolic pathway of fats. leucine and isoleucine residues. Q. leucine and isoleucine. Indole group. while glucogenic amino acids enter the pathway of glucose metabolism. Phenol group is present in which amino acid? (Page 12) A. Name a purely ketogenic amino acid. Q. What is the basis of classification of amino acids into ketogenic and glucogenic? (Page 12 and 13) A. Glycine. Q.10 Viva—based on Textbook of Biochemistry Q. serine. Tyrosine. A. Pyrrolidine group is present in which amino acid? (Page 12) A. Valine. Q. (Page 13) (Page 12) .(Page 12) A. Hydrophobic bonds are formed in protein between which amino acids? A. A. Q. Imidazole group. aspartic acid. Leucine. Which special group is present in Histidine? (Page 12) A. Valine.
Q. two are semi-essential and the rest 10 are non-essential. but they can be synthesized by the body and need not be essentially present in the diet (Page 14). it is synthesized from phenyl alanine. Q. But they are not essential for the adult individual. Is phenyl alanine an essential amino acid? (Page 13) A. Yes. Histidine and arginine. Name the semi-essential amino acids. threonine. (Page 14) A. Q. Why are they called semi-essential? (Page 14) A. Are non-essential amino acids necessary for the body? A. Q. and so. Hydroxyproline (Page 12). (Page 13) A. Q. Which amino acid is synthesised after it gets incorporated into the protein? A. They are also necessary for protein synthesis. . Because growing children require them in food. What about Tyrosine? (Page 13) A. How many amino acids are essential? (Page 13) A. What are essential amino acids? (Page 13) A. they are to be provided in the diet.Amino Acids: Structure and Properties 11 Q. Isoleucine. Q. Eight amino acids are essential. Tyrosine is non-essential. leucine. They cannot be synthesized in the body. Q. Q. Name any three essential amino acids.
What is iso-electric point?. Q. The pK value of Histidine is 6. (Page 14) A. What are natural amino acids? (Page 16) A. and therefore effective as a buffer at the physiological pH of 7.12 Viva—based on Textbook of Biochemistry Q. there is no mobility in electrical field. Glycine. the tendency for precipitation will be maximum Q. (Page 15) . Which is the amino acid having maximum buffering capacity at physiological pH? (Page 14) A. (Page 14) A. Which amino acid is optically inactive? A. Q. Histidine.1. What are the isomers of amino acids? (Page 16) A. Q. Q. The pH at which the molecule carries no net charge is called iso-electric point. What are the characteristic features of iso-electric pH. Only L amino acids are seen in large quantities in nature. D and L varieties. Q. At iso-electric point the amino acid will carry no net charge. What is the speciality of Histidine? (Page 14) A.4. The buffering capacity of plasma proteins and hemoglobin is mainly due to histidine residue. solubility will be minimum.
What is meant by decarboxylation of an amino acid? (Page 16) A. Q. Gamma amino butyric acid or GABA. Q. Aspartic acid + ammonia will form asparagine. Q. What is an amide? (Page 16) A. Q. The extra carboxyl group (other thanÿalpha carboxyl) can combine with ammonia to form the corresponding amide.Amino Acids: Structure and Properties 13 Q.8). Histidine to histamine. What is produced when Glutamic acid is decarboxylated? (Page 16) A. tyrosine to tyramine. actinomycin-D and valinomycin (Page 16). That is the amide of glutamic acid. (Page 16) Q. polymyxin. . What is transamination? (Page 16) A.3. Can you name some substances where D-amino acids are seen? A. What is glutamine? A.3. The carboxyl group is removed from the amino acids to form the corresponding amine (Fig. D-amino acids are seen in cell walls of micro-organisms and as constituents of certain antibiotics such as gramicidin-S. tryptophan to tryptamine. How asparagines is produced? (Page 16) A.10). The alpha amino group of amino acid can be transferred to alpha keto acid to form the corresponding new amino acid and alpha keto acid (Fig. Q. Q. Give examples of decarboxylation reactions. (Page 16) A.
Transaminases in blood are elevated in liver and heart diseases. Non-essential amino acids are synthesized by this process (Page 16). What is the significance of SH groups in proteins? (Page 17) A. (Page 16) A. Q. Phosphorylation is taking place on which amino acid residue? A. The SH group of cysteine can form a disulfide (SS) bond with another cysteine residue. Glutamic acid. Q. What is the clinical significance of transaminases? (Page 16) A. cysteine and glycine. Alanine and alpha keto glutarate (Page 16). Q. These are important for the interconversion of amino acids. Q. Glutamic acid + pyruvic acid alpha keto glutarate + alanine. Q. What is the biological significance of transamination reaction? A. The two cysteine residues can connect two polypeptide chains by the formation of interchain disulfide bonds. . Q. Glutathione is made up of which amino acids? (Page 17) A. Give an example of transamination reaction. What is the product of transamination reaction of pyruvate with glutamate? A. Serine (Page 17).14 Viva—based on Textbook of Biochemistry Q.
a condensation product of two urea molecules. . No. What is biuret reaction? (Page 18) A. Proteins do not give a true color reaction. Q. What is the use of biuret reaction? (Page 18) A. Do proteins give a color with ninhydrin? (Page 18) A. Q. Q. to produce a blue color. This reaction can be used for qualitative identification and quantitative estimation of proteins. It is often used for detection of amino acids in chromatography. The name is derived from the compound biuret. It is used for qualitative test and quantitative estimation of amino acids.Amino Acids: Structure and Properties 15 Q. but Nterminal end amino group of protein will react with ninhydrin. Will amino acids give a positive biuret test? (Page 18) A. This needs a minimum of two peptide bonds. All amino acids when heated with ninhydrin will give a pink colour. Cupric ions in alkaline medium form a violet colour with peptide bond nitrogen. Q. Q. What is the importance of ninhydrin reaction? (Page 18) A. What is biuret? (Page 18) A. which also gives a positive color test. What is ninhydrin reaction? (Page 18) A. Q.
Q.16 Viva—based on Textbook of Biochemistry Q. The ring systems in phenyl alanine. tyrosine and tryptophan will answer this test. . What is the basis of xanthoproteic test? (Page 18) A. (Page 18) A. The protein which does not answer the aldehyde test is. Gelatin.
A tripeptide is a combination of three amino acids. Q. Q. 4. Q. How many peptide bonds are present in a tripeptide? (Page 19) A. What is a dipeptide? (Page 19) A. Two amino acids are combined to form a dipeptide.1). What is a polypeptide? (Page 19) A. Alpha carboxyl group of one amino acid reacts with alpha amino group of another amino acid to form a peptide bond or CO-NH bridge (Fig. Proteins are made by polymerisation of amino acids through peptide bonds. Q. . How proteins are made up of? (Page 19) A. so there are two peptide bonds.Proteins: Structure and Function 17 Proteins: Structure and Function Q. What is a peptide bond? (Page 19) A. A combination of 10 to 50 amino acids is called as a polypeptide.
tertiary and quaternary levels of organisation. chains containing more than 50 amino acids are called proteins. Q. Proteins have primary. Q. What are the salient features of a peptide bond? (Page 19) A. at one end there will be one free alpha amino group.2). . A combination of 10 to 50 amino acids is called a polypeptide. Q. What is the N-terminal end of a protein? (Page 20) A. The C-N bond is ‘trans’ in nature and there is no freedom of rotation because of the partial double bond character. This end is called the amino terminal (N-terminal) end and the amino acid contributing the ?-amino group is named as the first amino acid. By convention. What are the levels of organizations of proteins? (Page 19) A. The primary structure is maintained by the covalent bonds of the peptide linkages (Fig. What is meant by primary structure of a protein? (Page 19) A. What is the force that maintains the primary structure? (Page 19) A. secondary. What is the difference between a polypeptide and a protein? (Page 19) A. Q. It denotes the number and sequence of amino acids in the protein. 4. The peptide bond is a partial double bond.18 Viva—based on Textbook of Biochemistry Q. In a protein. Q.
What are the names for the end amino acids of proteins. Insulin has total 51 amino acids. The end where there is a free alpha amino group is called the amino terminal (N-terminal) end. Q. Can you give an example of a pseudopeptide? (Page 20) A. These chains are held together by disulfide bridges. Q. .Proteins: Structure and Function 19 Q. Amino acid change in the linear sequence is called a mutation. What is mutation? (Page 20) A. other than that of alpha position. What are the salient structural features of insulin? (Page 20) A. What is the defect in HbS? (Page 20) A. The pseudopeptide a peptide bond formed by carboxyl group. Glutathione (gamma-glutamyl-cysteinyl-glycine). Q. Normally the 6th amino acid in the beta chain is glutamic acid. Q. (Page 20) A. sickle cell anemia due to Haemoglobin S. Q. The other end of the polypeptide chain is called the carboxy terminal end (C-terminal) where there is a free alpha carboxyl group. What is pro-insulin? (Page 20) A. Q. It has two polypeptide chains. Insulin is synthesised by the beta cells of pancreas as a prohormone. Can you give an example? (Page 20) A. this is replaced by valine in the HbS molecule. proinsulin is a single poly-peptide chain with 86 amino acids.
tertiary and quaternary structures of a protein? (Page 21) A. In other words. . secondary level defines the organisation at immediate vicinity of amino acids. The tertiary structure denotes three dimensional structure of the whole protein. Q. It is the term used to denote a compact unit of a protein. Van der Waal’s forces and Hydrophobic bonds. Which will inhibit the formation of alpha helix? (Page 22) A. Proline. it is major structural motif in globular proteins. What are the salient features of alpha structure of proteins? (Page 22) A. Hydrogen bonds. Which are the forces that maintain the secondary. What is meant by a domain of a protein? (Page 22) A. Q. It generally represents a functional unit. What is meant by secondary structure of a protein? (Page 22) A. Secondary structure denotes the configurational relationship between residues which are about 34 amino acids apart.6 amino acid residues. Q. Q. Q. Electrostatic bonds. What is meant by tertiary structure of a protein? (Page 22) A. It is a right-handed spiral structure.20 Viva—based on Textbook of Biochemistry Q. It defines the steric relationship of amino acids which are far apart from each other in the linear sequence. each turn is formed by 3.
the number of anions and cations present on the protein molecule will be equal and the net charge is zero. Finger printing of proteins or peptide mapping. optical rotatory dispersion. Q. At the iso-electric point. followed by two dimensional chromatography. Hemoglobin. Q. What is iso-electric point of a protein? (Page 25) A. and nuclear magnetic resonance (NMR). (Page 23) A. It is otherwise known as what? (Page 24) A. Protein chains may be separated by what reagent? (Page 24) A. Give some examples of proteins having quaternary structure.Proteins: Structure and Function 21 Q. X-ray diffraction study. Q. dansyl chloride. What is meant by Ingram’s technique?(Page 24) A. Secondary structure of protein can be studied by what methods? (Page 25) A. What are the reagents that are used for identifying the first amino acid in a protein? (Page 24) A. lactate dehydrogenase. 8 molar urea. Q. immunoglobulin. . Q. phenyl iso thio cyanate. Q. This is referred to as the quaternary structure. Fluoro dinitro benzene. Q. Certain polypeptides will aggregate to form one functional protein. What is meant by quaternary structure of a protein? (Page 22) A. Protein digestion by trypsin.
Give an example of precipitation at iso-electric point. . Q. Q.7. What is the iso-electric pH of human albumin? (Page 25) A. Globulins are precipitated by half-saturation of ammonium sulfate. solubility. Any factor which neutralises the charge or removes water of hydration will cause precipitation of proteins. the proteins will not migrate in an electrical field.6. buffering capacity and viscosity will be minimum and precipitation will be maximum. What will be precipitated by half-saturation of ammonium sulfate? (Page 25) A. By full saturation of ammonium sulfate or 28 % sodium sulfate. (Page 26) A. How albumin is precipitated? (Page 25) A. At the pI value. Q.22 Viva—based on Textbook of Biochemistry Q. What are the characteristic features of iso-electric point? (Page 25) A. 4. Casein is precipitated when the solution is brought to iso-electric pH. How proteins are precipitated from solution? (Page 25) A. What is the iso-electric pH of casein? (Page 26) A. Q. It is 4. Q. Q.
Brief heating. vigorous shaking. urea. high pressure. Albumin is easily coagulated. Give some examples of anionic precipitating agents. Q. Q. They may be classified depending on the function or based on the physicochemical characteristics or based on their nutritional value. Tungstic acid. Q. The denature proteins are insoluble and easily precipitated. (Page 26) A.Proteins: Structure and Function 23 Q. trichloro acetic acid. How proteins are classified? (Page 27) A. What is heat coagulation? (Page 26) A. What are the usual agents that cause denaturation of proteins? (Page 26) A. The functional activity is lost. phosphotungstic acid. Give examples of proteins that coagulate easily. . Q. This is called heat coagulation. some proteins will denature irreversibly to produce thick floating conglomerates called coagulum. What are the features of denaturation?(Page 26) A. The secondary. (Page 26) A. picric acid. sulphosalicylic acid and tannic acid are protein precipitating agents. but primary structure is preserved. ultraviolet ray. When heated at iso-electric point. X-ray. and globulins to a lesser extent. tertiary and quaternary structures are lost. Q.
nail and hoof. Q. chromoproteins.24 Viva—based on Textbook of Biochemistry Q. What are conjugated proteins? (Page 27) A. 6. What is the functional classification of proteins? (Page 27) A. (Page 27) A. Combinations of protein with a non-protein part is called prosthetic group. Give examples of simple proteins. 5. lipoproteins. flavoproteins. and 7. 4. Glycoproteins. scleroproteins. Regulatory proteins or hormones. Hemoglobin. Q. 3. keratin of hair. phospho-proteins and metallo-proteins. how are they classified? (Page 27) A. Give examples of scleroproteins. protamines. Structural proteins. nucleoproteins. globulins. prolamines. 1. Q. Protective proteins. 2. conjugated proteins and derived proteins. Catalytic proteins. horn. (Page 27) A. Genetic proteins. Contractile proteins. visual purple. cartilage and tendon. Q. (Page 27) A. Transport proteins. Q. . Simple proteins. Give some examples of chromoproteins. How are conjugated group subclassified? (Page 27) A. Based on physiochemical properties. lectins. Collagen of bone. Q. Albumins.
The phosphoric acid is added to the hydroxyl groups of serine and threonine residues of proteins. (Page 28) . Casein of milk and vitellin of egg yolk. Give an example of nutritionally poor protein. They lack in many essential amino acids and a diet based on these proteins will not even sustain the body weight. What are lectins? (Page 27) A. Which method of protein estimation is dependent on the intact peptide bond? A. Q.Proteins: Structure and Function 25 Q. Q. Q. Plant proteins having specific carbohydrate binding site. Give an example of a nutritionally rich protein (first class protein). Biuret method. why? (Page 28) A. Where is this phosphate attached to proteins? (Page 27) A. Q. Q. Give examples of phosphoproteins. Zein from corn lacks tryptophan and lysine. (Page 28) A. Some proteins are called as poor proteins. (Page 28) A. A. Casein. (Page 27) Q.
The sensitivity of the method is less and is unsuitable for estimation of proteins in milligram or microgram quantities. This is based on the reduction of folin-ciocalteau phenol reagent (phosphomolybdic acid and phosphotungstic acid) by the tyrosine and tryptophan residues of protein. .26 Viva—based on Textbook of Biochemistry Q. Q. What is nephelometry? (Page 29) A. Q. Nephelometry is defined as the detection of light scattered by turbid particles in solution. What is the disadvantage of biuret method? (Page 28) A. Q. Which component of the protein absorb UV light at 280 nm? (Page 28) A. What is the advantage of biuret method? (Page 28) A. Indole ring of tryptophan. The biuret method is simple one step process. and is the most widely used method for plasma protein estimations. Q. What is the basis of Lowry’s method of protein estimation? (Page 28) A.
What is the function of transferases? (Page 31) A. What is the function of hydrolases? A. hydrolases. What is the function of oxidoreductases? (Page 30) A. transferases. Give an example of oxidoreducatase. What are those classes? (Page 30) A. Cleave bond after adding water. Q. Oxidoreductases. A. Give an example of transferase. Q. They are classified into five major classes. Transfer of hydrogen. Q. isomerases and ligases. Q. Q.Enzymology-I 27 Enzymology-I Q. Transfer of groups other than hydrogen. Alcohol dehydrogenase. lyases. Hexokinase. (Page 31) (Page 31) . Q. (Page 30) A. How are enzymes classified? (Page 30) A.
Q. Cleave bond without adding water. Peptidases are classified under which class of enzyme? (Page 31) A. Which enzyme will add water to a double bond. Q. ATP dependent condensation of two molecules. without breaking the bond? A. (Page 31) Q. What is the difference between synthase and synthetase? (Page 31) A. Carbamoyl phosphate synthetase.28 Viva—based on Textbook of Biochemistry Q. Hydratase. Hydrolases. Give examples of synthetases. Give an example of a hydrolase. A. Synthases are enzymes catalysing biosynthetic reactions. glutamine synthetase. Give an example of lyase. Aldolase. (Page 31) Q. (Page 31) (Page 31) Q. A. A. . PRPP synthetase. Q. Triose phosphate isomerase. arginino succinate synthetase. What is the function of lyases? A. they belong to classes other than Ligases. Give an example of isomerase. they belong to Ligases. Acetyl choline esterase. (Page 31) Q. but they do not require ATP directly. (Page 31) A. Q. What is the function of ligases? (Page 31) A. Synthetases are ATP-dependent enzymes catalysing biosynthetic reactions.
Q. (Page 31) A. Give examples of synthases. the coenzyme. Nicotinamide adenine dinucleotide. Q. Fully active enzyme is called Holo-enzyme.Enzymology-I 29 Q. Q. Q. Give some examples of co-enzymes involved in oxidoreductases. Enzyme may contain a non-protein part. NAD. Flavin adenine dinucleotide. without which the enzyme cannot exhibit any reaction. IMP synthase. Q. How are co-enzymes classified? (Page 31) A. What is holo-enzyme? (Page 31) A. (b) Those co-enzymes taking part in reactions transferring groups other than hydrogen. Glycogen synthase. What is the full form of NAD? A. (Page 32) (Page 32) . Q. A co-enzyme is a low molecular weight organic substance. FAD. What are co-enzymes? (Page 31) A. (a) Those taking part in reactions catalysed by oxidoreductases by donating or accepting hydrogen atoms or electrons. and so act as a co-substrate. Coenzyme accepts one of the products of the reaction. ALA synthase. The co-enzyme is essential for the biological activity of the enzyme. (Page 31) A. holo-enzyme is produced. When apo-enzyme and co-enzymes are added. NADP. What is FAD? A.
Name the enzymes containing copper. Q. Q. . What is the full form of ATP? A.(Page 33) A. (Page 32) Q. Q. Thiamine pyrophosphate. (Page 33) A. xanthine oxidase. Adenosine triphosphate. During the oxidation of food stuffs. peroxidase. Chloride ions activate which enzyme? (Page 33) A. Other reaction requiring energy are coupled with ATP. Which metal is required for the action of Kinases? (Page 33) A. Q. co-enzyme A. a part of which is stored as chemical energy in the form of ATP. Xanthine oxidase. cytochrome oxidase. energy is released. ATP. Name some iron containing enzymes. tyrosinase. Magnesium. Q.30 Viva—based on Textbook of Biochemistry Q. Give some examples of co-enzymes involved in reactions other than hydrogen transfer. Cytochrome oxidase. Amylase. biotin. Superoxide dismutase. Q. It is the energy currency in the body. (Page 32) A. catalase. What is the function of ATP? (Page 32) A. pyridoxal phosphate. Which enzyme contains molybdenum? (Page 33) A.
What is Fischer’s theory? (Page 34) A. The substrate induces conformational changes in the enzyme. Q. The enzyme combines with the substrate. Proteases (proteolytic enzymes) having a serine residue at its active center. Q. (Page 35) A. such that precise orientation of catalytic groups is effected. What is Michaelis-Menten Theory ? (Page 33) A. What is Koshland’s induced fit theory? (Page 34) A. how reactions are classified? (Page 36) A. Q. That area of the enzyme where catalysis occurs is referred to as active site or active center. . which immediately breaks down to the enzyme and the product.Enzymology-I 31 Q. chymotrypsin. Trypsin. thrombin. isothermic and endothermic reactions. It states that the three dimensional structure of the active site of the enzyme is complementary to the substrate. Q. Q. Thermodynamically. to form an enzyme-substrate complex. What is active site of an enzyme? (Page 35) A. enzyme and substrate fit each other like a key and its lock. Exothermic. Give an example of a serine protease. What is meant by serine proteases? (Page 35) A. It is otherwise called enzyme-substrate complex theory. Q. Thus.
temperature. What is Km value? (Page 37) A. Q. Q. Q. What is endergonic reaction? (Page 36) A. Glucose + ATP ® Glucose-6-Phosphate + ADP. Substrate concentration (expressed in moles/L) at half-maximal velocity is the Km value. What are the salient features of enzyme kinetics? (Page 36) A. Hexokinase reaction. They increase the chemical reaction. Enzymes lower activation energy. pH and presence of activators or inhibitors. e. and therefore reaction essentially goes to completion. Here energy is released from the reaction. converting urea to ammonia + CO2 + energy. Enzyme concentration. What are the factors influencing enzyme reaction? (Page 36) A. What is exothermic reaction? (Page 36) A. Q.g. Energy is consumed and external energy is to be supplied for these reactions.32 Viva—based on Textbook of Biochemistry Q. substrate concentration. It denotes that 50% of enzyme molecules are bound with substrate molecules at that particular substrate concentration . product concentration.g. e. but do not alter equilibrium of the reaction. In the body this is usually accomplished by coupling the endergonic reaction with an exergonic reaction. Q. urease enzyme. What does it indicate? (Page 37) A.
Study of Km value will also differentiate the competitive and non-competitive inhibitions. heat denaturation and consequent loss of tertiary structure of protein occurs. the lesser the numerical value of Km. Each enzyme has an optimum pH. Determination of Km value is also useful to understand the natural substrate of an enzyme. Km value is thus constant for an enzyme. Why it falls? (Page 39) A. Km denotes the affinity of enzyme to substrate. when temperature is more than 50ºC. The velocity of reaction increases when temperature is increased. The graph will show a bell-shaped curve.Enzymology-I 33 Q. reaches a maximum and then falls (Bell-shaped curve) Q. It is the characteristic feature of a particular enzyme for a specific substrate. Q. What is the effect of pH on the activity of an enzyme? (Page 39) A. Q. Thus. . What is its significance? (Page 37) A. the affinity of the enzyme for the substrate is more. What is the use of assessing the Km value of an enzyme? What is the application? (Page 38) A. What is the effect of temperature on enzyme velocity? (Page 39) A. Q. Km is independent of enzyme concentration. on both sides of which the velocity will be drastically reduced.
alkaline phosphatase (optimum pH 9-10) and Acid phosphatase (4-5). What is zymogen? (Page 39) A. What is the optimum pH of usual enzymes? (Page 39) A. Pepsin (optimum pH 1-2). . Q. The pH decides the charge on the amino acid residues at the active site. What is the explanation for the effect of pH? (Page 39) A. Q. The net charge on the enzyme protein would influence substrate binding and catalytic activity. Are there any important exceptions for this general rule? (Page 39) A. It is otherwise called pro-enzyme. the active trypsin is formed. This results in unmasking of the active centre. Inactive zymogen is activated by removal of a piece of the pro-enzyme. Give an example of zymogen is activated? (Page 39) A.34 Viva—based on Textbook of Biochemistry Q. and removal of a small polypeptide from trypsinogen. Q. By splitting a single peptide bond. Q. Usually enzymes have the optimum pH between 6 and 8.
Vmax is not changed. Q. suicide inhibition. Q. non-competitive inhibition. This prevents autolysis of cellular structural proteins. and so acts as an antibacterial agent. . and only after secretion into the alimentary canal. 3. (Page 40) A. Coagulation factors are seen in blood as zymogen form. (Page 40) A. dicoumarol inhibits vitamin K. Sulfonamide inhibits PABA incorporation in bacteria. Q. Gastro-intestinal enzymes are synthesised in the form of pro-enzymes. their activation takes place only when necessity arises. Methotrexate inhibits folate reductase system. 2. What are the different types of inhibitions of enzyme activity? (Page 39) A. they are activated. Competitive inhibition. Km is increased. This prevents intravascular coagulation. Malonate inhibits succinate dehydrogenase. 4. and allosteric regulation. Q. What is the significance of zymogen activation? (Page 39) A. Give examples of competitive inhibition. Competitive inhibitor is a structural analogue.Enzymology-I 35 Q. It is reversible. Give examples of clinical application of competitive inhibition. What are salient features of competitive inhibition? (Page 40) A.
Antidote to methanol poisoning is ethanol which is the natural substrate for alcohol dehydrogenase. Sulfhydryl group. 4. Non-competitive inhibitor has no structural similarity with the substrate. fluoride inhibits and enolase. e. The inhibitor makes use of the enzyme’s own reaction mechanism to inactivate it. Give examples of non-competitive inhibition. What is the mechanism of inhibitory action of Di-isopropyl fluoro phosphate? (Page 41) A. (Page 41) A. Q. 2. Q. What is suicide inhibition? (Page 42) A. It is generally not reversible 3. Q. Methanol is oxidised by alcohol dehydrogenase to formaldehyde which causes the acute toxicity. Km is not changed. acetylcholine esterase. Q. What is the immediate treatment for methanol poisoning? (Page 41) A. the structural analogue is converted to a more effective inhibitor with the help of the enzyme to be inhibited. It inhibits enzymes with serine in their active centres. What are the salient features of non-competitive inhibition? (Page 41) A. Q. Di-isopropyl fluoro phosphate inhibits trypsin. Iodo-acetate inhibits enzyme by reacting with which group at the active site of the enzyme? (Page 41) A. Vmax is reduced.36 Viva—based on Textbook of Biochemistry Q. . So ethanol is preferentially utilised.g. In suicide inhibition.
ALA synthase. Allosteric enzyme has one catalytic site where the substrate binds and another separate allosteric site where the modifier binds. (4) Vmax is reduced. Another example is Allopurinol which is oxidised by xanthine oxidase to alloxanthine that is a strong inhibitor of xanthine oxidase. What are the salient features of allosteric inhibition? (Page 43) A. (2) It is partially reversible when excess substrate is added. (5) Most allosteric enzymes possess quaternary structure. (Table 5. It means. What is covalent modification? (Page 43) A.7) A. Q.Enzymology-I 37 Q. What is allosteric inhibition? (Page 42) A. Give examples for allosteric inhibition. Q. Ornithine decarboxylase (ODC) is inhibited by difluro methyl ornithine (DFMO). (3) Km is usually increased. aspartyl trans-carbamoylase. either addition of a group to the enzyme protein by a covalent bond. HMG CoA reductase Q. or removal of a group by cleaving a covalent bond. (1) The inhibitor is not a substrate analogue. . They are made up of subunits. Mechanism based inactivation. Q. What is the other term for suicide inhibition? (Page 42) A. Give examples for suicide inhibition. Q. (Page 42) A.
ALA synthase is autoregulated by the heme by means of repression. Enzymes whose concentration in a cell is independent of inducer are called constitutive enzymes. Q. In humans. What is repression? (Page 44) A. (Page 44) A. the number of enzyme molecules is reduced in the presence of repressor molecule. whereas glycogen phosphorylase is active when phosphorylated. Give an example of induction. . What is meant by induction? (Page 44) A. What are constitutive enzymes? (Page 44) A. The key enzyme of heme synthesis. Tryptophan pyrrolase and transaminases are induced by glucocorticoids. Induction of lactose-utilising enzymes in the bacteria when the media contains lactose in the absence of glucose. Give some examples of covalent modification. Q. in the phosphorylated state. Give an example of repression. Glucokinase is induced by glucose. Q.38 Viva—based on Textbook of Biochemistry Q. (Page 44) A. Induction is effected at the level of DNA. Q. Q. ALA synthase is induced by barbiturates. The inducer will relieve the repression on the operator site and will remove the block on the biosynthesis of the enzyme molecules. Glycogen synthase is inactive. (Page 44) A. Repression acts at the gene level.
Give an example for absolute specificity. group specificity and streospecificity. . (Page 44) A. Give examples of multi-enzyme complexes. Q. Absolute specificity. Urea is the only substrate for urease. trypsin can hydrolyse peptide bonds formed by carboxyl groups of arginine or lysine residues. (Page 45) A. Give an example for group specificity. Q. pyruvate dehydrogenase. What are the types of specificity shown by enzymes? (Page 45) A. Fatty acid synthase. and alpha keto glutarate dehydrogenase. (Page 45) A. Q.Enzymology-I 39 Q.
They are actively secreted into plasma. km value. and have some functions in the blood. Q. inhibitor specificity. They are coming out from cells due to normal wear and tear. What is non-functional enzymes in plasma? (Page 46) A. Electrophoresis. heat stability. Q.40 Viva—based on Textbook of Biochemistry Enzymology-II Iso-Enzymes and Clinical Enzymology Q. What are iso-enzymes? (Page 46) A. . They have identical catalytic properties. Q. but differ in structure. enzymes of blood coagulation. How to differentiate iso-enzymes. They are physically distinct forms of the same enzyme activity. and tissue localization. For example. Which is a functional enzyme in plasma? (Page 46) A. (Page 46) A.
and any condition which causes necrosis of body cells. Q. H4. H2M2. Lactate dehydrogenase has how many iso-enzymes? (Page 47) A.Enzymology-II 41 Q. but are drastically increased during cell death (necrosis) or disease. Q. How do you further investigate for myocardial infarction? (Page 47) A. How do you separate LDH iso-enzymes in laboratory? (Page 47) A. Lactate dehydrogenase has how many polypeptide subunits? (Page 47) A.6. It is a tetramer. What is their clinical significance? (Page 46) A. Q. Q. Four. carcinomas. Five Q. All these five forms are seen in all persons. assays of these enzymes are very useful in diagnosis of diseases. Their normal levels in blood are very low. forming five iso-enzymes. H3M. leukemias. M3H and M4 varieties. Myocardial infarction. Therefore. hemolytic anemias. . muscular dystrophy. What are they? (Page 47) A. LDH level in blood is increased in which conditions? (Page 47) A. LDH-1 (H4) iso-enzyme is increased. By cellulose acetate electrophoresis at pH 8. Q.
Therefore. Q. What are the serum enzymes helpful in the diagnosis of myocardial infarction? A. Normally LDH-2 (H3M1) concentration in blood is greater than LDH-1 (H4). . three iso-enzymes are possible. Therefore.42 Viva—based on Textbook of Biochemistry Q. Myocardial infarction. and therefore CK has an advantage over LDH. Q. CK estimation is very useful to detect early cases. muscular dystrophies. but this pattern is reversed in myocardial infarction. creatine kinase (CK) CK MB iso-enzyme and aspartyl transaminase (AST). The CK level starts to rise within three hours of infarction. Q. the subunits are called B for brain and M for muscle. The CK level is not increased in hemolysis or in congestive cardiac failure. What are the iso-enzymes of CK? (Page 48) A. What is the advantage of CK estimation over LDH estimation to identify myocardial infarction? (Page 48) A. where ECG changes may be ambiguous. this is called flipped pattern. Creatine kinase (CK) level in serum is increased in which conditions? A. (Page 48) Q. CK is a dimer. Lactate dehydrogenase (LDH) H4 iso-enzyme. What is flipped pattern? (Page 47) A.
and malignancy in liver. Q. Cardiac Troponin I is released into the blood within four hours after the onset of cardiac symptoms. . peaks at 12-16 hours and remains elevated for 5-9 days post-infarction. one percent from brain (BB or CK1) and fifteen percent CKmt from mitochondria.Enzymology-II 43 Q. Moderate increase may be seen in chronic liver diseases such as cirrhosis. CTI is very useful as a marker at any time interval after the heart attack. Eighty percent of molecules in circulation are MM (CK3) variety of skeletal origin. Estimation of total CK is employed in muscular dystrophies and CK-MB iso-enzyme is estimated to identify myocardial infarction. What are the origins of the CK iso-enzymes? (Page 48) A. Q. Therefore. When do you estimate total CK and the iso-enzyme? (Page 48) A. Q. Rise in ALT levels may be noticed several days before clinical signs such as jaundice are manifested. It is significantly elevated in myocardial infarction and moderately elevated in liver diseases. Q. What is the significance of AST? (Page 48) A. What is the significance of ALT? (Page 49) A. It is 75% sensitive index for myocardial infarction. five percent in circulation are MB (CK2) from heart. Very high values are seen in acute hepatitis. What is the advantage of cardiac troponin I over other parameters to identify the myocardial infarction? (Page 48) A.
ALP. High levels may be noticed in obstructive jaundice or cholestasis. It is elevated in about 15% cases of carcinoma of lung. ALT. metastatic carcinoma of bone. rickets. osteomalacia. Six. Q. osteoblastoma. GGT. inhibited by phenylalanine. ALP level is increased in both liver and bone diseases. Q. liver and gut and then named as Regan isoenzyme or carcinoplacental iso-enzyme. how many iso-enzymes are present? (Page 49) A.44 Viva—based on Textbook of Biochemistry Q. It is of placental origin. Moderate increase is seen in hepatic diseases (infective hepatitis. but NTP is only in liver diseases. Estimation of gamma glutamyl transferase is useful to detect which condition? (Page 50) A. NTP. Alcohol abuse. For alkaline phosphatase. It is the iso-enzyme of alkaline phosphatase. why? (Page 49) A. alcoholic hepatitis). Alkaline phosphatase level in serum is elevated in which conditions? (Page 49) A. Q. Q. What are the enzymes useful in diagnosing liver pathology? (Page 50) A. What is Regan iso-enzyme? (Page 49) A. . Very high levels are seen in bone diseases such as Paget’s disease. It is said that nucleotide phosphatase (NTP) is a better index of obstructive liver disease than alkaline phosphatase (ALP). Q.
Neuron specific enolase (NSE) for cancers of neuro-endocrine origin. PSA is very specific for prostate carcinoma. Q. What are the enzymes useful as tumour markers? (Page 50) A. iso-enzyme study is helpful or not? (Page 50) A. Total acid phosphatase may increase in some other conditions also. Q. what are they? (Page 50) A. Prostate carcinoma. Serum acid phosphatase level is increased in which condition? (Page 50) A. (Page 50) A. in alcohol abuse. tartarate labile iso-enzyme of ACP and Prostate specific antigen (PSA) for prostate carcinoma. In such conditions. Q. In infective hepatitis. Q. Regan iso-enzyme of ALP for lung tumour. Prostate carcinoma. Q. Give the clinical implications of these enzymes. GGT level is increased. intravascular hemolysis. Yes. in obstructive jaundice. . secondary metastasis in bones.Enzymology-II 45 Q. What is the advantage of prostate specific antigen? (Page 50) A. tartarate labile iso-enzyme is specific for prostate carcinoma. ALP level is increased. per rectal examination. ALT level is increased.
prolonged apnea when succinyl choline is given as anesthetic drug. Which enzyme deficiency is inherited as Xlinked? (Page 50) A. Q. Drug induced hemolytic anemia. Succinyl choline apnoea. Name some enzymes that are used as therapeutic agents.46 Viva—based on Textbook of Biochemistry Q. How the deficiency of GPD is manifested? (Page 51) A. Amylase and lipase. and pepsin for indigestion. Q. Q. Pseudo-cholinesterase deficiency is manifested as what? (Page 50) A. Glucose-6-phosphate-dehydrogenase. (Page 52) A. Q. Acute pancreatitis can be diagnosed by estimating which enzymes? (Page 51) A. . Asparaginase for leukemia. streptokinase to dissolve clots.
Q. What are the types of electrophoresis? (Page 53) A. cellulose acetate. . Horizontal and vertical types. What are the factors affecting the mobility in electrophoresis? (Page 53) A. Q. Methods of Study of Metabolism 47 Methods of Separation and Purification of Biological Compounds. the pH of the medium. What are the supporting media used? (Page 53) A. Net charge on the particles (pI of proteins).Methods of Separation & Purification of Biological Compounds. The term refers to the movement of charged particles through an electrolyte when subjected to an electric field. Filter paper. What is meant by electrophoresis? (Page 53) A. agarose gel. and properties of the supporting medium. Q. Methods of Study of Metabolism Q. starch gel and polyacrylamide gel. strength of electrical field. mass and shape of the particles. agar gel.
48 Viva—based on Textbook of Biochemistry Q. Electrophoresis is commonly employed for what purpose in laboratory? A. For serum electrophoresis and to see abnormalities in serum protein concentrations. Q. What is the advantage of polyacrylamide gel? (Page 53) A. It has a molecular sieving effect and so separation is very efficient. Q. What is immuno-electrophoresis? (Page 54) A. Here electrophoretic separation is followed by an antigen-antibody reaction. Q. What is the principle of adsorption chromatography? (Page 54) A. separation is based on differences in adsorption at the surface of a solid stationary medium. Q. What is the principle of partition chromatography? (Page 55) A. the components of the mixture to be separated are partitioned between the two phases depending on the partition co-efficient (solubility) of the particular substances. Q. What are the common types of partition chromatography? (Page 55) A. Paper chromatography and thin layer chromatography. Q. What is the advantage of TLC over paper chromatography? (Page 55) A. TLC needs lesser time, and separation is more effective.
Methods of Separation & Purification of Biological Compounds, Methods of Study of Metabolism 49
Q. What is Rf value? (Page 56) A. It is the ratio of the distance travelled by the substance (solute) to the distance travelled by the solvent. The Rf value is a constant for a particular solvent system at a given temperature. Q. What is the basic principle of ion-exchange chromatography? (Page 56) A. Here, the separation is based on electrostatic attraction between charged molecules to oppositely charged groups on the ion exchange resins. Q. What is the principle of gel filtration chromatography? (Page 56) A. The separation is effected on the basis of the size of the molecules. It is otherwise called molecular sieving. Q. Give the principle of affinity chromatography. (Page 56) A. The technique is based on the high affinity of specific proteins for specific chemical groups. Q. Give an example of affinity chromatography. (Page 57) A. Separation and quantitation of glycated hemoglobin. Q. What is the quickest method for separation of proteins? (Page 58) A. HPLC.
50 Viva—based on Textbook of Biochemistry Q. What is the principle of ultracentrifugation? (Page 58) A. Large molecules can be sedimented at high centrifugal forces whereas small molecules cannot. Rate of sedimentation depends on the size, shape and density of solute particles. Q. What is Svedberg unit? (Page 57) A. Sedimentation constant is expressed in Svedberg (S) units. Q. What are the uses of ultracentrifugation? A. 1. Separation of subcellular organelles. 2. Separation of lipoproteins. 3. Determination of molecular weight of proteins. Q. What are the methods used to determine the molecular weight of proteins? A. (1) Ultracentrifugation, (2) Gel filtration and (c) PAGE (poly acrylamide gel electrophoresis). (Page 57) Q. What is the advantage of radio-immuno assay? (Page 57) A. Very small quantities of substances could be accurately measured. Q. What is the radio-active label used for RIA? (Page 58) A. Iodine-125. Q. What is the half life of Iodine-125? A. About 60 days. (Page 58)
Methods of Separation & Purification of Biological Compounds, Methods of Study of Metabolism 51
Q. What are the disadvantages of RIA, when compared to ELISA? (Page 58) A. 1. Since radio-isotopes are used, only approved laboratories could take up the assay. 2. The shelf life of the reagent is short. Q. What are the enzymes commonly used in ELISA technique. (Page 58) A. Alkaline phosphatase (ALP) and horse radish peroxidase (HRP).
52 Viva—based on Textbook of Biochemistry
Chemistry, Digestion and Absorption
Q. How carbohydrates are classified? (Page 61) A. Based on the number of the sugar units available, they are classified as monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Q. What is a monosaccharide? (Page 61) A. Molecules having only one actual or potential sugar group are called monosaccharides. Q. What is a polysaccharide? (Page 61) A. They contain more than 10 sugar units. Q. How are they combined together? A. Through glycosidic linkages. (Page 61)
Q. How are monosaccharides further classified? (Page 61) A. Sugars having aldehyde group are called aldoses and sugars with keto group are ketoses.
Q. Glucose. They are mirror images with reference to penultimate carbon atom. What is the difference between glucose and galactose? (Page 62) A. Name a few pentoses. Q. Penultimate carbon atom. Xylose. D variety of sugars are common in nature.3). They are different with regard to the H and OH groups at the 4th carbon atom. Q. What are pentoses? (Page 61) A. Which is the most common monosaccharide in the body? A. Name some important monosaccharides. Galactose is present in which food? (Page 62) A. fructose. A. .Carbohydrates-I 53 Q. Lactose contains galactose and glucose. (Page 61) A. Galactose is the 4th epimer of glucose (Fig. Q. Q. Arabinose. Monosaccharides with five carbon atoms. (Page 61) Q. What is the difference between D and L sugars? (Page 62) A. mannose. Glucose. (Page 62) Q.8. Q. galactose. Lactose is present in milk. Which isomer is common in nature? (Page 62) A. Which is the reference carbon atom in sugars? (Page 62) A. Ribose.
8. What is the difference between glucose and fructose? A. . Glucose is an aldohexose. (Fig. Anomerism is produced with reference with which carbon atom? (Page 62) A. Give an example. These are anomers.4). The difference lies in the spatial configuration with reference to the first carbon atom in aldoses and second carbon atom in ketoses.54 Viva—based on Textbook of Biochemistry Q. and fructose is a ketohexose. glucose and mannose are an epimeric pair which differ only with respect to carbon atom 2. Q. (Fig. galactose is the 4th epimer of glucose. 8.3). What is the basis of mutarotation? (Page 62) A. only in configuration with regard to a single carbon atom (other than the reference carbon atom). 8.4). It is due to the anomeric carbon atom. When sugars are different from one another. Q. Anomers are produced by the spatial configuration with reference to the first carbon atom in aldoses and second carbon atom in ketoses. Q. How alpha and beta forms of sugars are produced? (Page 62) A. Q. What is epimerism? (Page 62) A. (Fig. (Page 62) A. For example. Similarly. they are called epimers. Q.
Q. Name a ketose. A. Fructose.
Q. What is the principle of Benedict’s test? (Page 64) A. In alkaline medium, sugar will cause reduction of cupric ions, to form red coloured precipitate. Q. What is the composition of Benedict’s reagent. (Page 64) A. It contains sodium carbonate, copper sulfate and sodium citrate. In the alkaline medium provided by sodium carbonate, the copper remains as cupric hydroxide. Sodium citrate acts as a stabilising agent to prevent precipitation of cupric hydroxide. Q. Benedict’s test is commonly employed for what? (Page 64) A. To detect the presence of glucose in urine. Q. Name a few reducing sugars. A. Glucose, fructose, mannose. (Page 64)
Q. Keto group is non-reducing, but fructose reduces Benedict’s solution, what is the cause for this anomaly? (Fig. 8.10) A. In alkaline medium, ketone group is converted to aldehyde, through enediol formation. Q. In the case of sugars, which of the properties go hand in hand? A. Reducing property, osazone formation and mutarotation. (page 64)
56 Viva—based on Textbook of Biochemistry Q. Glucose and fructose will form identical osazones, why? A. The difference in glucose and fructose is dependent on the first and second carbon atoms, and this is masked by the osazone formation. (Page 64) Q. On oxidation of glucose, what are produced? (Page 64) A. Glucuronic acid, gluconic acid and glucosaccharic acid. Q. Reduction of glucose produces what? (Page 64) A. Sorbitol. Q. Name some deoxy sugars. (Page 66) A. Deoxy ribose, fucose (deoxy galactose). Q. Which is the stain used to identify deoxysugar? (Page 66) A. Feulgen staining. Q. Name some important disaccharides. (Page 67) A. Sucrose, lactose, maltose. Q. What is the glycosidic linkage in lactose? (Page 67) A. Beta 1-4 linkage. Q. What is the glycosidic linkage in sucrose? (Page 67) A. 1-2 linkage.
Q. Which disaccharide has no free aldehyde or ketone group? A. Sucrose. (Page 67) Q. Glucose and fructose are reducing sugars, but sucrose (containing glucose and fructose) is a non-reducing sugar, why? (Page 67) A. Because the glycosidic linkage in sucrose involves 1st carbon of glucose and 2nd carbon of fructose, so both reducing groups are masked. Q. Hydrolysis of maltose will give rise to what ? (Page 67) A. Two glucose units. Q. Which is the sugar found in milk? A. Lactose. (Page 67)
Q. What are the component monosaccharides of lactose? (Page 67) A. Galactose and glucose. Q. Sucrose consists of what monosaccharides? (Page 67) A. Glucose + fructose. Q. Name reducing disaccharides. A. Lactose and maltose. (Page 67)
Q. How polysaccharides are classified? (Page 68) A. Homopolysaccharides (homoglycans) and heteropolysaccharides (heteroglycans). Q. What is a homopolysaccharide? (Page 68) A. They are composed of single kind of monosaccharides.
58 Viva—based on Textbook of Biochemistry Q. Give examples of homopolysaccharides. (Page 68) A. Starch, and glycogen. Q. What are heteropolysaccharides? (Page 68) A. They are composed of two or more different monosaccharides. Q. What are the characteristics of glycogen? (Page 69) A. It is composed of glucose units. It is the stored form of carbohydrate in animal kingdom. It has a highly branched structure. Q. What is the reserve carbohydrate in plant kingdom? (Page 69) A. Starch. Q. What is the end product of action of pancreatic amylase on starch? (Page 69) A. Maltose. Q. Cellulose and starch are polysaccharides made of glucose, but cellulose cannot be digest by human beings, why? (Page 69) A. Cellulose contains beta 1,4 linkages, which cannot be digested by human enzymes. Q. What is inulin? (Page 69) A. It is a homopolysaccharide, composed of fructose units. Q. What is the use of inulin? (Page 69) A. It is used to find renal clearance and glomerular filtration rate.
Q. Give examples of heteropolysaccharides. (Page 70) A. Agar, hyaluronic acid, heparin, chondroitin sulfate. Q. What are mucopolysaccharides? (Page 70) A. They contain uronic acid and amino sugars. Q. Which heteropolysaccharide does not contain uronic acid? (Page 70) A. Keratan sulfate. Q. Hyaluronic acid is seen in which tissues? (Page 70) A. Connective tissue, synovial fluid, tendons, vitreous humor. Q. What is the difference between glycoprotein and mucoprotein? (Page 71) A. If the carbohydrate content is less than 10%, it is called a glycoprotein. If the carbohydrate content is more than 10% it is a mucoprotein. Q. The rate of absorption of sugars in intestine is highest for which monosaccharide? (Page 71) A. Absorption rate of galactose is more than glucose, while fructose is absorbed at a lesser rate than glucose. Q. Glucose is absorbed at the luminal side of gastro intestinal cells by which mechanism? (Page 72, and Fig. 8.30) A. Carrier mediated co-transport with sodium, named as sodium dependent glucose transporter (SGluT).
Glucose transporter type 2 (GluT2) (Fig. How glucose is released from intestinal cells into the blood stream? A. . Insulin induces these transporters.30). Q. In diabetes mellitus. It is the glucose transporter present in muscle and adipose tissues. for the controlled supply of insulin into blood stream. because GluT4 is reduced in insulin deficiency. Q. entry of glucose into muscle is decreased. What is the importance of GluT4? (Page 72) A. How glucose is taken up by cells from blood stream? (Page 72) A. In tissues GluT2 is involved in absorption of glucose from blood.8. Q. What is the glucose sensor in the beta cells of pancreas? (Page 72) A. GluT2 acts as the glucose sensor mechanism.60 Viva—based on Textbook of Biochemistry Q.
In this pathway. . anaerobic glycolysis forms the major source of energy in actively contracting muscles. lactate is produced. In which condition pyruvate is produced. Gluconeogenesis. When oxygen is lacking. glucose is converted to pyruvate or lactate. What is glycolysis? (Page 73) A. What is the significance of Glycolysis?(Page 73) A. and when lactate? (Page 73) A. along with production of a small quantity of energy. In aerobic condition pyruvate is produced. Glycolysis is the only source of energy in erythrocytes. It is the only pathway that is taking place in all the cells of the body. Glycogen Metabolism Q. Glycolysis. Moreover. Q. Q.Carbohydrates-II 61 Carbohydrates-II: Major Metabolic Pathways of Glucose.
Enolase. What is the importance of phospho fructokinase? (Page 74) A. 75) A. and Step 9. energy is produced during which steps? (Page 74.62 Viva—based on Textbook of Biochemistry Q. acts specifically on glucose. But glucokinase is present only in liver. Q. Q. . What is glucokinase? (Page 73) A. Fluoride ions inhibit which enzyme? (Page 75) A. During glycolysis. It is an irreversible reaction.6-bisphosphate. It is the key enzyme (rate limiting enzyme) of the pathway. What is hexokinase? (Page 73) A. Step 6.3-bis phospho glycerate to 3-phospho glycerate. Phospho enol pyruvate to pyruvate. Hexokinase is the first step in the glycolysis pathway. Q. 1. glyceraldehyde-3-phosphate to 1. Q. RBCs. and cancer cells. It phosphorylates glucose to glucose-6-phosphate. exercising muscle. Q. Which tissues prefer anaerobic glycolysis? (Page 73) A. Step 5. What is the substrate for aldolase reaction? (Page 74) A. and is active when glucose level in blood is increased after a food. Q.3bisphospho glycerate. The reaction is similar to hexokinase. Fructose-1.
Carbohydrates-II 63 Q. Q.11) Q. What are substrate level phosphorylations in glycolysis? (Page 75. Fluoride is used to prevent glycolysis. 76) A. Lactate dehydrogenase reaction. as preservative for blood before glucose estimation. . NAD is reduced to NADH in which reaction of glycolysis? (Page 75) A. But when oxygen is lacking. this NADH is reconverted to NAD+ by what mechanism? (Page 76) A. 9. As the end product of glycolysis. This can be done by oxygen. (See Fig. What is the purpose of lactic acid production under anaerobic conditions? A. Q. pyruvate and NADH are formed. NADH is oxidised to NAD in which reaction of glycolysis? (Page 76) A. Q. Glyceraldehyde-3-phosphate dehydrogenase reaction. NADH generated in the 5th step has to be oxidised to NAD+. What is the importance of the above inhibition? (Page 75) A. Q. During anaerobiasis.3-bisphospho glycerate kinase (step 6) and pyruvate kinase (step 9). the 5th step has to be coupled with the 10th step for regeneration of NAD. Lactate dehydrogenase reaction. 1.
. where it is oxidised to pyruvate. By this means. pyruvate and NADH are formed.6-bisphosphate. where it is made to pyruvate and then to glucose.9. Q. Q. Q. Glucocorticoids. Fructose-6phosphate.64 Viva—based on Textbook of Biochemistry Q. So. lactate is produced in muscle. ATP. this NADH is reconverted to NAD+ by what mechanism? (Page 76) A. Citrate. It is then taken up through gluconeogenesis pathway. it is transported to liver. Oxygen is limited in muscle. Why lactate is transported from muscle to liver? (Page 77) A. Fructose-2. What is Cori’s cycle? (Fig. the lactate is efficiently reutilised by the body.13) A. What is the purpose of Cori’s cycle? (Page 77) A. Q. and becomes glucose. This glucose can enter into blood and then taken to muscle. so lactic acid could not be made to pyruvate in muscle. AMP. This lactate diffuses into the blood. What are the activators of phospho fructo kinase? (Page 77. Oxygen. Q. What are the inhibitors of phosphofructokinase? (Page 77) A. or lactic acid cycle. Lactate then reaches liver. During aerobic conditions. This cycle is called Cori’s cycle. During exercise. As the end product of glycolysis. 78) A.
3-bisphospho glycerate? (Page 79) A. Q.3-BPG reduces the affinity towards oxygen. In aerobic glycolysis. 12 ATP. Q. What are key glycolytic enzymes? (Page 77. what is the net yield of ATP from one glucose molecule? (Page 78 and Table 9. Q. 2 ATP. . 38 ATP. the net yield from one glucose molecule is how much? (Page 78 and Table 9. Q. 78) A. Q. Pyruvate dehydrogenase.3) A. isocitrate dehydrogenase. What is the net yield of ATP from one glucose molecule during anaerobic glycolysis? (Page 78 and Table 9. What are the steps in which carbon dioxide is produced from a glucose molecule? (Page 80) A. What is the function of 2.4) A. 78) A.Carbohydrates-II 65 Q. During complete oxidation. Glucokinase. Phospho fructo kinase. Q.5) A. alpha keto glutarate dehydrogenase. 2. When combined with hemoglobin. What is the action of insulin on glycolysis? (Page 77. 8 ATP. Q. How many ATPs are generated per one rotation of the citric acid cycle? A. Insulin stimulates glycolysis. Pyruvate kinase.
It catalyses the reaction. why? (Page 80) A.20) A. Q. What is pyruvate kinase? (Fig. Lipoic acid. pyruvate to oxaloacetate. What is gluconeogenesis? (Page 81) A. FAD. phospho enol pyruvate to pyruvate. Q.66 Viva—based on Textbook of Biochemistry Q.19) A.20) A. rather than retaining glucose for blood sugar regulation? (Page 80) A. NAD. Pyruvate dehydrogenase is an irreversible reaction. Production of glucose from non-carbohydrate sources. 9. 9. What are the co-enzymes necessary for oxidative decarboxylation of pyruvate? (Page 80) A. There is no net synthesis of glucose from fatty acids. Pyruvate to acetyl CoA is a totally irreversible reaction. The enzyme catalysing the reaction. Pyruvate is converted to acetyl CoA by which enzyme? (Page 80) A. Q. The enzyme catalysing the reaction. Pyruvate dehydrogenate. 9. Which enzyme irreversibly channels glucose to energy production. Q. Q. What is pyruvate dehydrogenase? (Fig. What is pyruvate carboxylase? (Fig. Q. . Co-enzyme A. Q. Thiamine pyrophosphate. pyruvate to acetyl CoA.
Glucogenic amino acids and lactate.Carbohydrates-II 67 Q. How many ATP molecules are required to convert two molecules of pyruvate into glucose? (Page 82) A. why? (Page 82) A. Glucose-6-phosphatase is present only in liver. Q. Blood glucose level can be raised by gluconeogenesis only by liver. Biotin and ATP. Liver. Pyruvate carboxylase reaction (pyruvate to oxaloacetate) needs which co-enzyme? (Page 81) A. 83) A. Hence the oxaloacetate has to be transported from mitochondria to cytosol. This is achieved by the malate shuttle (see Fig. Gluconeogenesis is taking place in which tissue? (Page 81) A. Reactions of gluconeogenesis are taking place in cytosol. . Q. Q. Q. Fructose-1. Pyruvate carboxylase. Phospho enol pyruvate carboxy kinase. What are those non-carbohydrate sources? (What are the substrates for gluconeogenesis?). What are the key gluconeogenic enzymes? (Page 82) A. Q. (Page 82. Malate shuttle is used for what purpose? (Page 82) A. Q. 9.22). Six.6-bisphosphatase and Glucose-6-phosphatase.
. (Page 85) Q. Q.68 Viva—based on Textbook of Biochemistry Q. Insulin. Glycogen phosphorylase. Muscle glycogen will not serve as a precursor of blood sugar. What will inhibit gluconeogenesis? A. Gluconeogenesis is necessary to maintain blood glucose level especially under conditions of starvation. Degradation of glycogen to glucose. why? (Page 82) A. Which amino acids are both ketogenic and glucogenic? (Fig.29) A. Q. Glucagon and glucocorticoids. Q. Q. What is the main enzyme for glycogenolysis? (Page 86) A. Adrenaline and glucagon causes glycogenolysis. 9. Q. Glucose-6-phosphatase is absent in muscle. What is the significance of gluconeogenesis? (Page 85) A. Tyrosine and tryptophan. Q. Adrenaline increases cyclic AMP level which activates glycogen phosphorylase. What will stimulate gluconeogenesis? (Page 85) A. Which hormones enhance glycogenolysis? (Page 87) A. What is glycogenolysis? A. What is the mechanism of action of adrenaline? (Page 87) A. (Page 86) Q.
Epinephrine. cyclic AMP. Q. (Page 89) . Glucose-6-phosphatase. UDP-glucose. Which is the defective enzyme in von Gierke’s disease (glycogen storage disease type I)? (Page 89) A. Adrenaline acts on which enzyme? A. What will activate glycogen phosphorylase? (Page 87) A. glucagon. Q. which is the active glucose derivative? A. Glycogen phosphorylase. In the glycogen synthesis. which does not respond to adrenaline is very characteristic. Q.Carbohydrates-II 69 Q. Fasting hypoglycemia. Q. What are the characteristic clinical features of von Gierke’s disease? A.
Insulin decreases blood sugar. Q. enhances glycogen synthesis and inhibits lipolysis. growth hormone. (Page 90) Q. 70-110 mg/dl. Which hormone is hypoglycemic? A. inhibits glycolysis. . What are the anti-insulin (hyperglycemic) hormones? (Page 90) A. What are the major actions of glucagon? (Page 91) A. Glucagon. (Page 90) Q. Insulin. adrenaline. What are the major actions of insulin? (Page 90) A. Promotes glycogenolysis. Q. inhibits gluconeogenesis. depresses glycogen synthesis.70 Viva—based on Textbook of Biochemistry Carbohydrates-III: Regulation of Blood Sugar. enhances gluconeogenesis. What is the level of fasting blood sugar in a normal person? A. corticosteroids. it stimulates glycolysis. Insulin and Diabets Mellitus Q.
Seventy five gram anhydrous glucose (82. Fasting plasma sugar is more than 126 mg/dl. 3. Q.Carbohydrates-III 71 Q. Or. In order to prevent vomiting. patient is asked to drink it slowly (within about 5 minutes). on more than one occasion. What are the criteria for diagnosing diabetic mellitus? (Table 10. (Page 92) A. Q. . What are the precautions to take before OGTT? (Page 92) A. Q. Patient has symptoms suggestive of diabetes mellitus. Or. Patient should avoid insulin and oral antidiabetic drugs. Flavouring of the solution will also reduce the tendency to vomit. on the same occasion.1). Patient should not take any breakfast. if both fasting and 2hour values are above these levels. if 2-hour post-glucose load value of OGTT is more than 200 mg/dl (even at one occasion). Q. What is the glucose load dose? (Page 92) A. What is the major indication for doing an oral glucose tolerance test (OGTT)? (Page 92) A. Patient should fast overnight.5 g of glucose monohydrate) in 250-300 ml of water. What is the best method for glucose estimation? (Page 91) A. Patient should have a good carbohydrate diet for three days prior to the test. Glucose oxidase peroxidase (GOD-POD) method. 2. Q. but fasting blood sugar value is inconclusive (between 100 and 126 mg/dl). What precaution would you take in giving the glucose load? (Page 92) A.
Impaired glucose tolerance. What is impaired glucose tolerance (IGT)? (Page 93) A.72 Viva—based on Textbook of Biochemistry Q. Diabetes is diagnosed. Such persons need careful follow up because IGT progresses to frank diabetes at the rate of 2% patients per year. Diabetes mellitus. fasting plasma sugar is abnormal (between 110 and 126 mg/dl). Q. Diagnosis should not be based on a single random test alone. Q. (Page 93) A. What you will do for such persons? (Page 93) A. but the 2-hour post-glucose value is within normal limits (less than 140 mg/dl). on more than one occasion. 120 min = 160 mg / dl. . What is your diagnosis? A. Q. it should be repeated. if the random plasma sugar level is more than 200 mg/dl. What is impaired fasting glycemia (IFG). When a standard oral glucose tolerance test was done. What will be your diagnosis? (Page 92) A. the blood glucose levels of the patient were found as:0 min = 120 mg/dl. In this condition. When a standard oral glucose tolerance test was done. (Page 93) Q. Can you diagnose diabetes on the basis of random blood estimations? (Page 92) A. the blood glucose levels of the patient were found as:0 min = 130 mg/dl and 120 min = 220 mg /dl. Q. When fasting plasma glucose level is between 110 and 126 mg/dl and 2-hour post-glucose value is between 140 and 200 mg/dl.
Q. Women with GDM are at increased risk for subsequent development of frank diabetes.Carbohydrates-III 73 Q. What are other conditions which may cause impaired glucose tolerance? (Page 93) A. What is gestational diabetes mellitus (GDM)? (Page 93) A. but are to be kept under constant check-up. This term is used when carbohydrate intolerance is noticed. If a known diabetic patient. for the first time. during a pregnancy. Alimentary glucosuria. will you include her in the category of GDM? (Page 93) A. After the child birth. After delivery. Q. GDM is associated with increased birth weight of child and increased incidence of neonatal mortality. based on the results of a fresh OGTT. Q. Q. Q. the women should be re assessed and accordingly classified as having either diabetes mellitus or normal glucose tolerance. What is the clinical significance of GDM? (Page 93) A. No. . it is taken as gestational diabetes. renal glucosuria. These persons need no immediate treatment. what you will do for a person with GDM? (Page 93) A. who becomes pregnant. They are at increased risk for development of diabetes or cardiovascular diseases. If the fasting value is more than 126 mg%. What you will do for such persons? (Page 93) A.
What is lactosuria? (Page 94) A. Q. lactose. Q. But it is important to distinguish lactosuria from glucosuria when gestational diabetes mellitus is suspected. Here glucose is excreted in urine due to a lowering of renal threshold. glucuronides. fructose. . Excessive secretion of catecholamines will produce hyperglycemia and resultant glucosuria. The condition is harmless.74 Viva—based on Textbook of Biochemistry Q. It may occur in some people due to emotional stress.11. What is the clinical importance of lactosuria? (Page 94) A. Q. What are the reducing substances seen in urine? (Page 94) A. pentoses. It is observed in the urine of normal women during 3rd trimester of pregnancy and during lactation. Glucose. What is transient glucosuria? (Page 94) A. the glucosuria disappears. Q. ascorbic acid. Q. What is renal glucosuria? (Page 93) A. What is normal renal threshold for glucose? (Page 93) A.11). It is due to the deficiency of fructokinase or aldolase B (Fig. The blood sugar levels are within normal limits. Presence of fructose in urine. Q. galactose. Once theÿstress is removed. 180 mg/100 ml. What is fructosuria? (Page 94) A.
It is the part removed from proinsulin during the maturation of insulin molecule. glycogenolysis. Glucose-6-phosphatase. ketogenesis. glycogen phosphorylase. What is proinsulin? (Page 96) A. Beta cells of langerhans of pancreas. to form the A and B chains of insulin. HMP shunt pathway. acetyl CoA carboxylase. lipogenesis. Insulin is synthesised as a large single polypeptide. What is the test for reducing sugars in urine? (Page 95) A. glycogen synthesis. Middle part of it is then removed. Q. (Page 96) Q. Q. Gluconeogenesis. Phospho fructo kinase.Carbohydrates-III 75 Q. glucose-6-phosphate dehydrogenase. What is C peptide? (Page 96) A. (Page 96) A. . Where is insulin synthesised? A. Benedict’s test. What are the important enzymes inhibited by insulin? (Page 96) A. glycogen synthase. lipolysis. Glycolysis. Q. Q. Q. Q. What are the pathways inhibited by insulin? (Page 96) A. What are the pathways stimulated by insulin? (Page 96) A. Name important enzymes that are stimulated by Insulin. hormone sensitive lipase.
Glucose is the major stimulant of insulin secretion. . Then measurement of C-peptide is useful. Sometimes measurement of endogenous insulin may be difficult because of the presence of antibodies against insulin in the circulation. Q. Cyclic AMP along with calcium causes the insulin secretion. What is the clinical significance of C peptide? (Page 96) A. the A chain with 21 amino acids and the B chain with 30 amino acids are joined together by a pair of disulfide bonds.76 Viva—based on Textbook of Biochemistry Q. Q. Insulin facilitates the membrane transport of glucose in most of tissues. Insulin is a protein hormone with two poly peptide chains. Q. It has a total of 51 amino acids. This is by glucose transporter. How glucose stimulates insulin secretion? (Page 96) A. How is insulin secretion controlled? (Page 96) A. But glucose uptake by GlT2 is independent of insulin. it is seen in liver and brain. The insulin secretion is controlled by a cyclic AMP-mediated mechanism. The beta cells have GluT 2 receptors. Q. these act as sensor mechanism for glucose level. GIuT4. especially in muscles and adipose tissue. What are the salient structural features of insulin? (Page 96) A. What is the effect of insulin on glucose uptake of cells? (Page 97) A.
on the target cells. Q. (Page 99) Q. Here circulating insulin level is normal. Rapid loss of body weight is observed. Q. Insulin acts by binding to membrane receptor. What are the characteristic features of type 1. Type 1 and type 2. diabetes mellitus? A. The beta subunits are towards cytoplasmic side. but there is a relative insulin deficiency. How diabetes mellitus is classified? A. Maximum glucose utilisation is seen in which tissue? (Page 97) A. Q. What about type 2 diabetes mellitus? (Page 100) A. brain utilises 60% of sugar oxidised. Most of the patients belong to this type. These patients are dependent on insulin injections. Onset is during adolescence. Here circulating insulin level is deficient. Q. These patients are less prone to developing ketosis. At basal rates. The alpha units are located on the extracellular side.Carbohydrates-III 77 Q. two alpha and two beta subunits. . What is the structural feature of insulin receptor? (Page 97) A. Beta subunit has tyrosine kinase activity. to which insulin binds. It is commonly seen in individuals above 40 years. They are more prone to developing ketosis. What is the mechanism of action of insulin? (Page 97) A. Insulin receptor has four subunits.
What is maturity onset diabetes of young (MODY)? (Page 100) A. Keto acidosis. What are the acute complications of diabetes mellitus? (Page 100) A. thirst centre is activated. lactic acidosis. Q. patient takes more food. Q. more water accompanies the glucose. What are the cardinal symptoms of diabetes mellitus? (Page 100) A. hyperosmolar non-ketotic coma. What is the reason for polyuria in diabetes mellitus? (Page 100) A. To compensate the loss of glucose and protein. Q.78 Viva—based on Textbook of Biochemistry Q. and more water is taken (polydypsia). What is the reason for weight loss in diabetes mellitus? (Page 100) A. It is due to defective glucokinase. . Polyuria. Due to osmotic effect. What is the reason for polydypsia in diabetes mellitus? (Page 100) A. To compensate for this loss of water. Q. Q. polyphagia and weight loss. polydypsia. The loss and ineffective utilisation of glucose leads to breakdown of fat and protein. Q.ÿThis would lead to loss of weight. What is the reason for polyphagia in diabetes mellitus? (Page 100) A. When the blood glucose level exceeds the renal threshold glucose is excreted in urine.
What is micro-albuminuria? (Page 101) A. peripheral neuropathy. nephrosclerosis. What is the difference between glycosylation and glycation? A. proteins in the body may undergo glycation. Thrombosis. Albumin 50 to 300 mg/day in urine.Carbohydrates-III 79 Q. atherosclerotic diseases and cardiovascular mortality. What is the cause for cataract in diabetes mellitus? (Page 101) A. What are the chronic complications of diabetes mellitus? (Page 101) A. When there is hyperglycemia. micro-angiopathy. Early development of cataract of lens is due to the increased rate of sorbitol formation. (Page 101) Q. Enzymatic addition of any sugar to a protein is called “glycosylation” while non-enzymatic process is termed “glycation”. Q. Q. paralysis. What is the basis of glycation? (Page 101) A. It is a predictor of progressive renal damage. caused by the hyperglycemia. It is a non-enzymatic process. cataract. Glucose is added to the N-terminal amino group of proteins. gangrene. Albumin more than 300 mg/day indicates overt diabetic nephropathy. Q. .
. An elevated glycohemoglobin indicates poor control of diabetes mellitus. It is unaffected by recent food intake or recent changes in blood sugar levels. but for monitoring the response of treatment.80 Viva—based on Textbook of Biochemistry Q. The determination of glycated hemoglobin is not for diagnosis of diabetes mellitus. What is the significance of glycated hemoglobin? (Page 101) A. The risk of retinopathy and renal complications are proportionately increased with elevated glycatedhemoglobin.
Galactose. What is the hormonal control over HMP shunt pathway? (Page 103) A. Alcohol) Q. ovary. Glucuronic Acid. Which is the key enzyme of hexose monophosphate shunt pathway? (Page 103) A. RBC.Carbohydrates-IV 81 Carbohydrates-IV: Other Metabolic Pathways (HMP Shunt Pathway. mammary gland. . Liver. Glucose-6-phosphate dehydrogenase. adipose tissue. adrenal cortex. Q. Q. HMP shunt pathway use how much glucose? (Page 103) A. testis. Q. Insulin stimulates the pathway by activating the key enzyme. Fructose. lens. What are the tissues in which HMP shunt pathway is significant? (Page 103) A. About 10% of glucose molecules per day are entering in this pathway.
What is the use of NADPH in biological systems? (Page 105) A. Q. is there any other purpose for the HMPshunt pathway? (Page 106) A. Q. Q.82 Viva—based on Textbook of Biochemistry Q. it is needed for keeping glutathione in reduced state. What reductive biosynthesis pathways need NADPH? (Page 105) A. NADPH is not used for ATP generation. The pathway is required for the synthesis of ribose. it is necessary for superoxide production inside macrophages. It generates NADPH. it is required for keeping transparency of lens. Apart from NADPH generation. steroid hormones. Apart from reductive synthesis. synthesis of cholesterol. It is necessary to keep the integrity of RBC membrane. . What about ATP generation? NADPH is used for that? (Page 106) A. Q. NADPH is used for what purpose? (Page 105) A. What is the purpose of HMP shunt pathway? (Page 104) A. Which enzyme generates NADPH? (Page 103) A. Q. Fatty acid biosynthesis. For reductive biosynthesis. Glucose-6-phosphate dehydrogenase. No. the pentose phosphates are necessary for nucleotide (DNA and RNA) synthesis. Q.
Deficiency of glucose-6-phosphate dehydrogenase. Acute hemolytic episode after administration of antimalarial drug is due to what? (Page 106) A. . The transketolase reaction is measured in RBCs as an index of the thiamine status of an individual. Q.Carbohydrates-IV 83 Q. It occurs owing to the enzyme having low binding capacity for TPP. What is the most common enzyme deficiency in man? (Page 106) A. Q. Q. What is the mode of hereditary transmission of GPD deficiency? (Page 106) A. Q. The geographical distribution of GPD deficiency correlates well with the malarial endemicity. Drug induced hemolysis and met-hemoglobinemia. The occurrence of Wernick’s encephalopathy (seen in alcoholics and in thiamine deficiency) is due to a genetic defect in the enzyme transketolase. Is there any advantage of the abnormal gene? (Page 106) A. What is the clinical significance of transketolase enzyme? (Page 107) A. It is transmitted as an x-linked recessive character. Abnormal transketolase leads to what clinical condition? (Page 107) A. Glucose-6-phosphate dehydrogenase deficiency. The GPD deficiency offers resistance to malarial infection. What is the manifestation of glucose-6-phosphate dehydrogenase deficiency? (Page 106) A. Q. Q.
Q. Q. But it gives a positive reaction to Benedict’s test. What is the purpose of uronic acid pathway? (Page 107) A. For synthesis of ascorbic acid (vitamin C). steroids. What is fructose intolerance? (Page 108) A. uronic acid pathway is used for what purpose? (Page 107) A. This leads to accumulation of glycogen in liver. fructose-1-phosphate accumulates. Thiamine pyrophosphate (TPP). Q. It does not produce any harm. Q. In lower animals. Fructokinase catalyses which reaction? (Page 108) A.84 Viva—based on Textbook of Biochemistry Q. Q. . synthesis of gluco-saminoglycans. What is the clinical significance of polyol pathway? (Page 107) A. Q. What is its importance? (Page 107) A. Transketolase activity is decreased in the deficiency what? (Page 107) A. and hypoglycemia. The elevated level of sorbitol has been implicated in the development of neuropathy. Excretion of pentose (L-xylulose) in urine due to the deficiency of xylitol dehydrogenase. so it should be differentiated from diabetes mellitus. Q. Fructose to fructose-1-phosphate. Due defective aldolase-B. What is essential pentosuria? (Page 107) A. cataract and retinopathy in diabetes mellitus. It is used for conjugation of bilirubin.
Q. Fructose is secreted by seminal vesicles. Polyol pathway of glucose. A block in seminal vessels is indicated by the absence of fructose in semen. Q. This fructose is produced by which pathway? (Page 107) A. and so it should be differentiated from diabetes mellitus. Seminal plasma. Q. Free fructose is seen in which body fluid? (Page 108) A. What is the clinical application of fructose estimation in semen? (Page 108) A.Carbohydrates-IV 85 Q. hepatosplenomegaly. Galactosemia. fructose intolerance. Q. Urine gives positive Benedict’s test. neonatal hypoglycemia. Congenital cataract is seen in which condition? (Page 109) A. Q. galactosemia. It is a benign metabolic defect due to deficiency of fructokinase. type I. Q. . positive Benedict’s test. Congenital cataract. What is fructosuria? (Page 108) A. What are the features of galactosemia? (Page 109) A. Neonatal hypoglycemia is seen in which conditions? (Page 109) A. Glycogen storage disease. mental retardation.
Lactose free diet is given for first five years of life. Werneck’s encephalopathy. Because ethanol inhibits gluconeogenesis. Q. the alternate pathway (galatose-1phosphate pyrophosphorylase) becomes active. . During alcohol oxidation. Galactose-1-phosphate uridyl transferase. Q. Galactosemia is due the absence of which enzyme? (Page 109) A. why life-long treatment is not required? (Page 110) A. Q. Why excessive intake of alcohol produces hypoglycemia? (Page 110) A. Q. which converts pyruvate to lactate. How N-acetyl neuraminic acid (sialic acid) is synthesised? (Page 111) A. Q. N-acetyl mannosamine-6-phosphate + phospho enol pyruvate. Polyneuropathy. Q.86 Viva—based on Textbook of Biochemistry Q. cirrhosis. Why five years. fatty liver. What are the results of chronic alcoholism? (Page 111) A. By five years. NADH is generated. What is the treatment policy in galactosemia? (Page 110) A. Why excessive intake of alcohol produces lactic acidosis? (Page 110) A.
Increased glucosaminoglycans in urine is seen in which condition? (Page 113) A. In glycoproteins.Carbohydrates-IV 87 Q. Mucopolysaccharidosis. Q. . Hydroxyl group of serine or threonine. carbohydrate residues are attached to which group of the polypeptide chain? (Page 112) A.
compound and derived. . Even chain fatty acids. (Page 115) A. Simple. Mainly Oleic acid. Which type is prevalent in human body? (Page 115) A. How lipids are classified? A. Classify fatty acids. What fatty acids are generally present in human fat? (Page 116) A. Digestion and Absorption of Lipids Q. Depending on the total number of carbon atoms. they are classified as even chain and odd chain. Fatty acids are classified in any other manner? (Page 116) A. Q.88 Viva—based on Textbook of Biochemistry Lipids-I: Chemistry. They are also classified as saturated or unsaturated fatty acids. then comes palmitic acid and linoleic acid. (Page 115) Q. Q. Q.
18 carbon. What is the structure of linolenic acid? (Page 117) A. Which contains good quantity of PUFA? (Page 118) A. with two double bonds. Q. ground nut oil. linolenic and arachidonic acids. Vegetable oils such as sunflower oil. Oleic. linoleic.Lipids-I 89 Q. 18 carbon. Linoleic. Coconut oil and animal fats. Name some unsaturated fatty acids. How many carbon atoms are present in oleic acid? (Page 116) A. with one double bond. Q. Q. (Page 117) A. What is the structure of linoleic acid? A. 20 carbon with four double bonds. Name some polyunsaturated fatty acids. Q. (Page 117) A. linolenic and arachidonic acids. 18 carbon with three double bonds. Q. Q. What is the structure of arachidonic acid? (Page 117) A. Which contains very low level of PUFA? (Page 118) A. (Page 117) . Q.
Pancreatic lipase. Does saponification number of a fat molecule increase or decrease with the molecular weight of the fat? (Page 119) A. Hydrolysis of fat by alkali is called are saponification. Partial oxidation of fatty acids. The products are 2-mono acylglycerol (2-MAG) (?-monoglyceride) and two fatty acid molecule (Fig. . Partial hydrolysis of triacyl glycerol. Q. storage does not require water. Decreases with increase in molecular weight of fat. Complete digestion of triacyl glycerol (triglyceride) in gastro intestinal tract needs what enzymes? (Page 120) A. Space requirement is less. isomerase and bile salts Q. Q. Q.90 Viva—based on Textbook of Biochemistry Q.7). can be mobilised whenever required. What is the function of pancreatic lipase? (Page 120) A. with formation of epoxides and peroxides of small molecular weight fatty acids. co-lipase. capacity for storage is unlimited. What is the advantage of storing energy as triglycerides in the body? (Page 119) A. 12. Q. What is saponification? (Page 119) A. Odour of rancid oil is due to what? (Page 119) A.
Q. What are the final end products of digestion of triglyceride? (Page 120) A. Q. Isomerase shifts the ester bond from position 2 to 1. Will there be complete breakdown of triglyceride into fatty acid in the gastro intestinal tract? (Page 120) A. only partial digestion is possible. What is the chemical name of bile salts? (Page 120) A. Q. 1-monoacyl glyceride (6%). By emulsifying the lipids and producing micelles of lipids. Long chain fatty acids (chain length more than 14 carbons) are absorbed by forming micelles with the help of bile salts. How small chain fatty acids are absorbed? (Page 120) A. Q. 2-monoacyl glyceride (78%). Q. How bile salts help in the absorption of dietary lipids? (Page 120) A. What is the function of isomerase? (Page 120) A. Sodium glycocholate and sodium taurocholate. .Lipids-I 91 Q. glycerol and fatty acids (14%). this is then hydrolysed by the lipase to form free glycerol and fatty acid. Q. No. Small chain and medium chain fatty acids (chain length less than 14 carbons) are directly absorbed from the intestinal lumen into the portal vein and taken to the liver. How long chain fatty acids are absorbed? (Page 120) A.
along with phospholipids. The chyle (milky fluid) from the intestinal mucosal cells loaded with chylomicrons are transported through the lacteals into the thoracic duct and then emptied into systemic circulation.92 Viva—based on Textbook of Biochemistry Q. What is the difference for absorption of short chain fatty acid? (Page 120) A. phospholipids and lysophospholipids are incorporated into molecular aggregates to form mixed micelles. the long chain fatty acids are re-esterified to form triglycerides (Fig. The triglyceride. Monoglycerides. Once inside the intestinal mucosal cell. Q.9). Short and medium chain fatty acids do not need re-esterification. Q. What is the further fate of this triglyceride? (Page 121) A. apoproteins B48. Fatty acids and monoacyl glycerides from the micelles passively diffuse into the mucosal cell. The micelles are spherical particles with a hydrophilic exterior and hydrophobic interior core (Fig. .8). 12. What happens to the micelles? (Page 120) A. and apo-A are incorporated into chylomicrons. Q. They directly enter into blood vessels (Not to lacteals). Q. long chain fatty acids. cholesterol. What are micelles? (Page 120) A.12. What happens to the fatty acids in the mucosal cell? (Page 120) A.
e. When excretion of fat in faeces is more than 6 g per day. It may be due to diseases in intestinal mucosa.g. The bile salts are left behind. If the absorption alone is defective. Q. What happens to the bile salts of micelle? (Page 120) A. It is due to defective digestion as in chronic diseases of pancreas. i. They are separately reabsorbed from the ileum and returned to the liver to be re-excreted again to gut. unsplit fat is excreted in feces. fatty acids and monoglycerides. sprue. coeliac disease. What is the cause for defective absorption of fat? (Page 121) A. What is steatorrhea? (Page 121) A. most of the fat in faeces may be split fat. . Q. coconut oil and mother’s milk. What happens in defective absorption? (Page 121) A. ghee. Q. In such cases. Q. Crohn’s disease. What is enterohepatic circulation of bile salts? (Page 120) A. it is called steatorrhea.e. Q.Lipids-I 93 Q. Q. Where will you find short and medium chain fatty acids? (Page 120) A. What is it due to? (Page 121) A. They are seen in butter.
tumours of head of pancreas. enlarged lymph glands.94 Viva—based on Textbook of Biochemistry Q. Since milk fat and coconut oil are made up of MCT. etc. triglycerides with short chain and medium chain fatty acids are digested and absorbed properly. they are therapeutically useful in malabsorption syndromes. . Q. Any condition leading to a deficiency of bile salts can also result in malabsorption of fat. The most common causes are obstruction to biliary tract due to gall stones. In such cases. because they do not require micellerisation for absorption. What is the line of management in defective absorption? (Page 121) A. Any other cause for defective absorption of fat? (Page 121) A.
Ketone bodies.Lipids-II 95 Lipids-II: Metabolism of Fatty acids. Fatty acid oxidation. . How fatty acids are activated in preparation of oxidation? (Page 122) A. Q. Thus two high energy bonds are utilised in this reaction. Fatty acids are activated to their co-enzyme A (CoA) derivative. Thiokinase or fatty acyl CoA synthetase. Q. Lipolysis. What are the co-enzymes needed for fatty acid oxidation? (Page 122) A. One molecule of ATP is hydrolysed to AMP and PPI. FAD and NAD. What is the enzyme for this activation? (Page 122) A. Q. Q. Fatty acid synthesis. How much ATP is required for this reaction? (Page 122) A.
when one molecule of palmitic acid (16 carbon) is oxidised completely? (Page 123) A. . It is synthesised from lysine and methionine in liver and kidney. so they are easily oxidised. Q.96 Viva—based on Textbook of Biochemistry Q. and NADH. Therefore a transporter. What are the energy producing steps in beta oxidation pathway? (Page 123) A. Medium chain fatty acids do not require carnitine for transport. during each cycle of beta oxidation of fatty acid? (Page 123) A. Propionyl CoA. Carnitine is beta-hydroxy-gamma-trimethyl ammonium butyrate. What is the net generation of ATP. What is the product of beta oxidation of odd chain fatty acids? (Page 124) A. Q. Acetyl CoA. What about medium and small chain fatty acids? (Page 122) A. Q. 129. Fatty acyl CoA dehydrogenase (FAD) and beta hydroxy fatty acyl CoA dehydrogenase (NAD) steps. FADH2. Q. What is carnitine? (Page 122) A. What is the function of carnitine? (Page 122) A. but the beta-oxidation is in mitochondria. Q. Q. What are the products. Fatty acids are activated in the cytoplasm. carnitine is involved in transfer of fatty acids. The long chain fatty acyl CoA cannot pass through the inner mitochondrial membrane.
and oxidation in TCA cycle. Q. from the carboxyl end. activation of acetoacetate. Q. What is alpha oxidation of fatty acid?(Page 124) A. Propionyl CoA is first carboxylated to methyl malonyl CoA and then to form succinyl CoA. Q. Q. valine. Q. Refsum’s disease is due to what? (Page 125) A. Biotin. What is the further metabolism of propionyl CoA? (Page 124) A. The succinyl CoA then enters TCA cycle. Where is alpha oxidation taking place? (Page 124) A. In endoplasmic reticulum (microsomes). Porphyrin biosynthesis. ATP. threonine. due to defective alpha oxidation. Alpha oxidation does not generate energy. one at a time. Odd chain fatty acids. Accumulation of phytanic acid. Succinyl CoA is generated from which substances? (Page 124) A. It is a process by which fatty acids are oxidised by removing carbon atoms. It is used for fatty acids that have a methyl group at the beta-carbon. What are the co-enzymes required for the conversion of propionyl CoA to succinyl CoA? (Page 124) A. which blocks beta-oxidation. propionic acid. Vitamin B12. . Q. isoleucine. Succinyl CoA is utilised for what purposes? (Page 124) A.Lipids-II 97 Q.
What are the co-enzymes required for the reaction? (Page 126) A. NAD and FAD are necessary. Q. ATP citrate lyase. Q. Q. In the HMP shunt pathway. Acetyl CoA carboxylase. Biotin and ATP. . fatty acid synthesis is in cytoplasm. by which enzyme? (Page 126) A. synthetic enzymes are grouped as a multi-enzyme complex. Q. Q. Acetyl CoA from mitochondria is transferred to cytoplasm for the de novo synthesis of fatty acid. for synthesis. What are the steps in which NADPH is used in fatty acid synthesis? (Page 127) A. Beta oxidation is taking place in mitochondria. Step 4 (Keto acyl reductase) and Step 6 (Enoyl reductase). Acetyl CoA + CO2 ® Malonyl CoA. What is the reaction? (Page 126) A. What are the major differences between fatty acid synthesis and beta oxidation of fatty acid? (Page 125) A. What is the rate limiting enzyme of de novo synthesis of fatty acid? (Page 126) A. Q. 2 carbon units are added as 3 carbon malonyl CoA.98 Viva—based on Textbook of Biochemistry Q. during synthesis. How NADPH is made available? (Page 128) A. 2 carbon units are removed as acetyl CoA. For oxidation. During oxidation. Oxidation enzymes are independent. NADPH is used. glucose-6-phosphate dehydrogenase reaction produces NADPH.
3). malic enzyme. cytoplasmic malate dehydrogenase. availability of acetyl CoA is increased. Insulin enhances the uptake of glucose by adipocytes and increases the activity of pyruvate dehydrogenase. so that enough NADPH is available. What are the sources of NADPH for fatty acid synthesis? (Page 128) A. Insulin favours lipogenesis. How? (Page 128) A. cholesterol synthesis and ketone body formation. Q.13. . Chain elongation of fatty acid is taking place in which site? (Page 128) A. oxidation in citric acid cycle for generation of energy.Lipids-II 99 Q. Q. What is the action of insulin on fatty acid synthesis? (Page 128) A. So. Fatty acid synthesis. is stimulated by citrate and inhibited by palmitoyl CoA. the key enzyme of fatty acid synthesis pathway. Moreover. Glucose-6-phosphate dehydrogenase. Microsomal elongation system is more active. Key enzyme.11). Acetyl CoA is used for what purposes? (Page 127) A. Q. Q. Insulin also depresses the hormone sensitive lipase (Fig. Q. insulin stimulates acetyl CoA carboxylase. How is fatty acid synthesis regulated? (Page 128) A. (Table 10. Insulin also activates glucose-6-phosphate dehydrogenase. acetyl CoA carboxylase.
corticosteroids. and glucagon. hormone sensitive lipase hydrolyses triglyceride into fatty acid and releases into blood. Q. In adipose tissue. derived from glucose. Q. What is its action? (Page 129) A. Q. Thermogenesis. What enzyme is involved in lipolysis? (Page 129) A. In adipose tissue. White adipose tissue is concerned with what? (Page 129) A. Energy storage. Insulin. Q. In the blood. adrenalin. Q. what is the source of glycerol phosphate for triglyceride formation?(Page 129) A. Q. By hormone sensitive lipase. Albumin is the carrier of free fatty acid. Triacyl glycerol synthesis is enhanced by which hormone? (Page 129) A. ACTH. From dihydroxy acetone phosphate. fatty acids are transported as what form? A. Hormone sensitive lipase is activated by which hormones? (Page 129) A. Growth hormone. Q. Brown adipose tissue is involved in what process? (Page 129) A. .100 Viva—based on Textbook of Biochemistry Q.
cyclic AMP and kinase. Growth hormone. What are ketone bodies? (Page 131) A. It inhibits phospho diesterase. and so. What are the sources of acetyl CoA? (Page 130) A. Alcohol. . What is the mechanism of activation of hormone sensitive lipase? (Page 129) A. Pyruvate. non-esterified fatty acid level in blood is increased. corticosteroids. this inhibition is removed. why? (Page 129) A. Q. diabetes mellitus. Q. Q. Q. more lipolysis is taking place. methionine. Choline. Q. hepatitis virus. in diabetes. excess calorie intake. In diabetes mellitus. caffeine favours lipolysis. Insulin inhibits hormone sensitive lipase. so. and acetone. and glucagon. Aceto acetate. What is the action of caffeine? (Page 129) A. beta hydroxy butyric acid. acetoacetyl CoA. What worsens fatty liver? (Page 130) A. Which are the lipolytic hormones? (Page 129) A. ACTH. lecithin. What substances will prevent fatty liver? (Page 131) A. Q. adrenalin. prolongs the action of cyclic AMP. Thus. Q. and leucine. A cascade through adenyl cyclase. increases activity of hormone sensitive lipase. fatty acids.Lipids-II 101 Q.
Step 1: Absence of insulin leads to excessive hydrolysis of triacyl glycerol. . mevalonate. except liver). Q. The excess acetyl CoA is diverted into ketone body formation. (All other tissues. Mitochondria. Ketogenesis is taking place in which subcellular organelle? (Page 131) A. Q. Q. Q. What is the rate-limiting-step in ketone body formation? (Page 131) A. Ketolysis is taking place in extra hepatic tissues. Liver. HMGCoA synthase. Q. Q. Utilisation of ketone bodies by peripheral tissues needs which enzyme? (Page 131) A. Q. Ketone body utilisation is taking place in which organs? (Page 131) A. Ketone bodies are formed in which tissue? (Page 131) A. What test is used to identify ketone bodies in urine? (Page 132) A. HMGCoA is directly converted into what substances? (Page 131) A. and more acetyl CoA is produced. Succinyl CoA dependent thiophorase.102 Viva—based on Textbook of Biochemistry Q. Rothera’s test. acetyl CoA. Step 2: So more fatty acid is available. Acetoacetate. Step 3: But oxidation of acetyl CoA in citric acid cycle is sluggish. Ketosis is due to what processes? (Page 132) A.
It has 27 carbon atoms. . Glucocorticoids. Q. Q. Which food stuffs contain cholesterol? (Page 133) A. testosterone. mineralocorticoids. Lipoproteins and Cardiovascular Diseases Q. Non-vegetarian food. Q. Q. Cholesterol has how many carbon atoms? (Page 133) A. bile acids. What are the substances derived from cholesterol? (Page 133) A. Whether cholesterol is present in vegetable oils? (Page 133) A. No. estrogen. What is the ring structure present in cholesterol? (Page 133) A. Perhydro cyclo pentano phenanthrene ring.Lipids-III 103 Lipids-III: Cholesterol.
and partly as bile salts. What is the first sterol ring formed during cholesterol biosynthesis? (Page 134) A. Either by electrophoresis or by ultracentrifugation. What is the normal level of triglycerides? (Page 135) A. HMG CoA reductase. What is HMG CoA synthase? (Page 131) A. Lanosterol. Through bile. What is the rate-limiting-step in the cholesterol biosynthesis? (Page 134) A. Q. What is the normal level of total plasma lipids? (Page 135) A. How cholesterol is excreted? (Page 135) A. HDL (alpha lipoprotein). 150-220 mg/dl. How lipoproteins are estimated? (Page 136) A. It is the rate-limiting-enzyme in ketogenesis pathway. During electrophoresis. Q. partly as cholesterol itself. Q. Q. What is the normal level of total cholesterol? (Page 135) A. Q. Q. Q. what is the fastest moving lipoprotein? (Page 136) A. 50-200 mg/dl.104 Viva—based on Textbook of Biochemistry Q. Q. 400-600 mg/dl. .
B48. what is the least moving lipoprotein? (Page 136) A. What is the function of chylomicron? (Page 137) A. Q. but not in liver. Q. Lipoprotein lipase. muscles and heart. It is located at the endothelial layer of capillaries of adipose tissue. During electrophoresis.Lipids-III 105 Q. Highest content of triglycerides is seen in which lipoprotein? (Page 137) A. Q. What is the main apoprotein present in LDL? (Page 138) A. LDL (Beta lipoprotein). B100. VLDL. (Page 137) A. Q. Q. Triglycerides present in chylomicrons are hydrolysed by what? (Page 137) A. Maximum cholesterol content is in which lipoprotein? (Page 136) A. Q. Endogenous triglycerides in plasma are carried by what? (Page 138) A. Transport of triglycerides from intestine to adipose tissue. it is the ligand for LDL receptor. Where is the enzyme present? (Page 137) A. Chylomicrons. . Q. Q. Chylomicron (gamma position). What is the main apoprotein present in chylomicron.
What is lipoprotein(a) ? (Page 139) A. What is the function of LDL? (Page 138) A. (Page 139) Q. the receptor-LDL complex is internalised by endocytosis. What is the significance of lipoprotein (a)? (Page 139) A. Lp(a) is associated with heart attacks at the age of 30 or 40 years. Q. Why it is called so? (Page 139) A. LDL receptors are present on all cells but most abundant in hepatic cells and adrenal cortex. Q.10). and causes atherosclerosis. LDL transports cholesterol from liver to peripheral tissues. Indians have a higher level of Lp(a) than Europeans. What is the function of LDL receptors? (Page 138) A. where it is deposited. What is “bad cholesterol”? A. It is attached to apo B-100 by a disulfide bond. located in specialised regions called clathrin-coated pits. When the apo B-100 binds to the receptor.106 Viva—based on Textbook of Biochemistry Q. LDL cholesterol. It has significant homology with plasminogen.14. Q. This leads to unopposed intravascular thrombosis and possible myocardial infarction. LDL receptors. . Q. So it interferes with plasminogen activation and impairs fibrinolysis (Fig. Transport of cholesterol from liver to peripheral tissues.
What is LCAT? (Page 139) A. Q. Q. Lecithin cholesterol acyl transferase. Q. What is the normal level of lipoprotein (a) ? (Page 139) A. Why it is called so? (Page 139) A. Apo A-1. In 40% population. and so helps in excretion of cholesterol from the body. HDL transports cholesterol from peripheral tissues to liver. What is “good cholesterol”? A. there is no detectable level of Lp(a) in serum. So HDL is anti-atherogenic. LCAT present in plasma is activated by apo-A1. What is the main apoprotein present in HDL? (Page 139) A. and these persons are susceptible to heart attack at a younger age. Q. it is the ligand for HDL receptor. HDL cholesterol. . What is the function of HDL? (Page 139) A. LCAT is necessary. The free cholesterol is esterified by LCAT the esterified cholesterol is then incorporated into HDL disc.Lipids-III 107 Q. What is its importance? (Page 139) A. Q. to form mature HDL. Q. Transport of cholesterol from peripheral tissues to liver. Where is it present? (Page 139) A. In 20% of population. (Page 139) Q. So for excretion of cholesterol. the Lp(a) concentration in blood is more than 30 mg/dl. when LCAT binds to HDL disc.
Free fatty acids of plasma are bound to what? (Page 140) A. Q. Q. What are the salient features of hyperlipoproteinemia Type II-A? (Page 141) A. Transport of free fatty acid from adipose tissue to peripheral tissues. (Page 141) Q. Premature atherosclerosis elevated plasma LDL cholesterol. The esterified cholesterol is then taken by HDL. Triglycerides present in adipose tissue are hydrolysed by what enzyme? (Page 140) A. increased intake of PUFA. and prominent beta band on electrophoresis. Hormone sensitive lipase. What is the treatment policy? (Page 141) A.108 Viva—based on Textbook of Biochemistry Q. Defect in LDL receptor. for excretion of cholesterol. and finally excreted through liver. What is the importance of PUFA in cholesterol metabolsim? (Page 140) A. Q. What is it due to? A. PUFA is required. What is the function of albumin? (Page 140) A. PUFA will lower the blood level of cholesterol. Q. So. PUFA present in lecithin is transferred to cholesterol by the enzyme LCAT. . bile acid binding resins. Low cholesterol diet. Q. Thus. Bound to serum albumin. decreased intake of saturated fat.
How LDL deposit leads to atherosclerosis? (Page 143) A. Q. What happens to atherosclerotic plaque? (Page 143) A. Oxidised LDLcholesterol is deposited in the subintimal regions of arteries. the macrophages become overloaded with cholesterol esters. 150-220 mg/dl. Diabetes mellitus. Oxidised LDL is taken up by macrophages. This leads to narrowing of vessel wall. Hypercholesterolemia is seen in what conditions? (Page 143) A. Q. What tissues are affected mostly by atherosclerosis? (Page 143) A. nephrotic syndrome. obstructive jaundice. this is due to liberation of various growth factors. . What is the normal serum cholesterol level? (Page 142) A. and these are then called “foam cells” which form the hallmark of atherosclerotic plaques. Q. Aorta. Again a clot is formed which occludes one of the major vessels. How atherosclerosis started? (Page 143) A. Then there is ischemia of the tissue supplied. Finally infarction or ischemic death of the tissue occurs. hypothyroidism. Q. coronary arteries and cerebral vessels are predominantly affected.Lipids-III 109 Q. The effect is directly proportional to the LDL levels. Q. Free radical induced oxidative damage of LDL will accelerate this process. Then fibrous proliferation takes place.
What advise you will give to a person with increased cholesterol level? (Page 144) A. Q. Q. When patient’s condition is not responding to the dietary restriction. HMGCoA reductase inhibitors. avoid cigarettes. What are the drugs available to treat hypercholesterolemia? (Page 144) A. fibrate derivatives. exercise. LDLcholesterol level above 160 mg/dl. nicotinic acid. reduction of total fat intake of green leafy vegetables. homocysteine level. diabetes mellitus. Cigarette smoking. hypertension. Q. What are the important risk factors of coronary artery diseases? (Page 144) A. Bile acid binding recins. Q. Q. and Apo(a) above 30 mg/dl. . include PUFA and omega-3 fatty acids in diet. What is the function of bile acids? (Page 146) A. obesity. sedentary life style. When will you start drugs for a person with increased cholesterol level? (Page 144) A. Serum cholesterol level above 220 mg/dl. They are the major route of excretion of cholesterol and they are required for absorption of triacyl glycerol. HDL-cholesterol level below 35 mg/dl. Reduce food with higher cholesterol content of food.110 Viva—based on Textbook of Biochemistry Q. What are other risk factors associated with coronary artery diseases? (Page 144) A. serum triglyceride level above 200 mg/dl.
Bile acids conjugated with taurine or glycine. Q.Lipids-III 111 Q. How are bile salts formed? (Page 146) A. Cholesterol. Bile acids are derived from what substance? (Page 146) A. .
What is the difference in digestion of MCT from that of LCFA? A. PUFA and Prostaglandins Q. Medium chain fatty acids they contain 8 to 14 carbon atoms.112 Viva—based on Textbook of Biochemistry Lipids-IV: MCFA. Pancreatic lipase and bile salts are not required. (Page 147) . Very long chain fatty acids they contain 20 or more carbon atoms. MCT containing triglycerides are digested by MCT-specific lipase. Long chain fatty acids they contain 16 to 18 carbon atoms. Q. What is MCFA? (Page 147) A. Q. What is LCFA? (Page 147) A. Q. What is VLCFA? (Page 147) A.
MCFA are easily digested. So what is the advantage of MCFA? (Page 147) A. Because. 127. Further. When palmitoleic acid (16 C. Q. when compared to the corresponding chain length saturated fatty acid. (Page 147) Q. Name polyunsaturated fatty acids. and easily oxidised (when compared to LCFA). 1 double bond) is completely oxidised. easily absorbed. MCFA is carried by albumin in blood. (Page 147) A. Q. So they are to be provided in the diet. What is the difference in absorption of MCFA from that of LCFA? A. (Page 147) Q. what is the net generation of ATP molecules? (Page 147) A. Q. Why 2 ATP molecules are reduced? (Page 147) A. The energy yield is less by 2 ATP molecules per double bond. the FAD dependent dehydrogenation (step 1 of beta oxidation) does not occur at the double bond. Q. as in the case of LCFA). Those cannot be synthesised by the body. linolenic and arachidonic acids.Lipids-IV 113 Q. MCFA is absorbed directly to blood (not to lacteals. after absorption. whereas LCFA are absorbed as triglycerides and carried by chilomicrons. Linoleic. What are essential fatty acids? (Page 148) A. When unsaturated fatty acids are oxidised. . how many ATP is formed? A.
According to the attachment of different substituent groups to the ring. What is the enzyme called? A. (Page 148) A. e. This is the most common variety. PGE2. leukotienes. Q. Q. The Series 2 (with two double bonds) are derived from arachidonic acid. thromboxanes. Prostaglandins. Q. Prostaglandins are derived from what substance? (Page 149) A. synthesis of phospholipids and esterification of cholesterol. etc. Q. (Page 148) Q. depending on number of double bonds on the side chains they are denoted by a subscript after the capital letter. Where does desaturation of fatty acid takes place? (Page 148) A. What are the important substances derived from PUFA? (Page 148) A. What are the functions of PUFA? (Page 148) A.114 Viva—based on Textbook of Biochemistry Q. PGs are named with capital letters such as A. Synthesis of prostaglandins. How prostaglandins are classified? (Page 149) A. B.g. Series 2 have two double bonds at 13-14 (trans) and 5-6 (cis). HPETE. In the same series. Microsomal desaturase system. PGE1. In the endoplasmic reticulum. prostacycline. All naturally occurring PGs belong to the 2-series. Name the essential fatty acids. E and F. Prostaglandins are derived from the PUFA. . Q. Linoleic and linolenic acids are the only fatty acids which cannot be synthesised in the body. PGE3.
. Prostaglandins are stored in what form? (Page 149) A. Prostaglandins have only very short half life. Q. How prostaglandin synthesis is regulated? (Page 150) A. What is the mechanism of action of aspirin? (Page 150) A. How prostaglandins are synthesised?(Page 149) A. The arachidonic acid is released by the action of phospholipase A2 on phospholipids prostaglandin synthesis is catalysed by prostaglandin H synthase (PGHS). It contains two separate enzyme activities. Steroids inhibit PL and prevent release of arachidonic acid from membranes. as membrane phospholipids. They are inactivated by the 15hydroxy-prostaglandin-dehydrogenase which converts 15-OH group to keto group. Q. Aspirin acetylates serine in the active site and irreversibly inhibits the cyclo-oxygenase.Lipids-IV 115 Q. The phospholipase is activated by epinephrine. Q. Cyclo-oxygenase is a “suicide” enzyme. Cyclo-oxygenase is activated by catecholamines and inhibited by non-steroid anti-inflammatory drugs (NSAIDS). cyclo-oxygenase and peroxidase. Q. What is the importance of cyclo-oxygenase? (Page 150) A. As precursors. Q. How is prostaglandins inactivated? (Page 150) A. of about 30 seconds.
They are produced from arachidonic acid. constrict the bronchioles. Thromboxane (TXA2) is the main PG produced by platelets. PGE increases cAMP level.116 Viva—based on Textbook of Biochemistry Q. What is the mechanism of action of prostaglandins? (Page 150) A. Q. it is the most potent chemotactic agent. But in adipose tissue and in renal tubular cells. What is the precursor of leukotrienes? (Page 151) A. Prostaglandins are local hormones. Q. increase capillary permeability and produce vasoconstriction. and function through G-protein coupled receptors In most tissues. It also inhibits platelet aggregation and has a protective effect on vessel wall against deposition of platelets. What is its biological importance? (Page 151) A. They cause smooth muscle contraction. Q. Prostacyclin and thromboxane are opposing in activity. What is the effect of thromboxane? (Page 150) A. PGE lowers cAMP level. LT B4 is produced in neutrophils. Q. Prostacyclin causes vasodilatation. What is the action of prostacyclin on vascular endothelium? (Page 150) A. The slow reacting substance of anaphylaxis (SRS-A) contains LTC4. The major effects are vasoconstriction and platelet aggregation. . LTD4 and LTE4.
DHA can be obtained from fish oils or from milk. Q. Eicosa penta-enoic acid (EPA) (Timnodonic acid. Fatty acids having 20 or more carbon atoms are called very long chain fatty acids (VLCFA). DHA is synthesised linolenic acid. 6 double bonds) are good examples of VLCFA. What are VLCFAs? (Page 151) A. DHA is especially required for the development of brain and retina. What is the importance of DHA? (Page 151) A. C-20. C-22. . Low levels of DHA in blood is seen in patients with retinitis pigmentosa.Lipids-IV 117 Q. 5 double bonds) and docosa hexa-enoic acid (DHA) (cervonic acid.
Phospho sphingosides 5. 2. Glycosphingolipids 6. What is phosphatidic acid? (Page 152) A. Non-nitrogen containing glycero phosphatides. Phosphatidic acid is made up of one glycerol to which two fatty acid residues are esterified to carbon atoms 1 and 2 and the 3rd hydroxyl group is esterified to a phosphoric acid. Q. 4. Phosphatidyl choline. Plasmalogens. Phosphatidyl ethanol amine. 3. Nitrogen containing glycero phosphatides. How phospholipids are classified? (Page 152) A. 1. (Page 152) .118 Viva—based on Textbook of Biochemistry Lipids-V: Compound Lipids Q. What is Lecithin? A. What is Cephalin? A. (Page 152) Q. Q. Sulpholipids.
Q. Q. phosphatidyl glycerol. . What is a globoside? A. Diphosphatidyl glycerol. (Page 154) (Page 154) Q. It contains choline. All sphingolipids have the long aliphatic aminoalcohol sphingosine which is attached to a fatty acid in amide linkage to form a ceramide. Low levels of surfactant leads to respiratory distress syndrome (RDS).Lipids-V 119 Q. B and C. What is lung surfactant? (Page 153) A. Sphingomyelins are the only sphingolipid that contain phosphate and have no sugar moiety. What is its clinical significance? (Page 153) A. Ceramide oligosaccharides. cholesterol and surfactant proteins A. A common phosphosphingoside present abundantly in the nervous system. Surfactant decreases surface tension of the aqueous layer of lung and prevents collapse of lung alveoli. Q. is sphingomyelin. Ceramide monohexoside. What is Cardiolipin? A. Surfactants contain dipalmitoyl lecithin. What are the constituents of surfactants? (Page 153) A. (Page 152) Q. What is a cerebroside? A. Q. It is produced by lung epithelial cells. What is sphingomyelin? (Page 154) A. which is a common cause of neonatal morbidity.
. choline. (Page 154) Q. Niemann Pick’s disease. Q. fatty acid. Q. Q. Gaucher’s disease. Tay Sach’s disease. (Page 156) A. Gaucher’s disease is due to the deficiency of what? (Page 157) A. A ganglioside on hydrolysis. Choline. Phospholipids can aggregate into what ? (Page 153) A. Glucocerebroside. What is accumulated in Gaucher’s disease? (Page 157) A. What is the nitrogenous base present in lecithin? (Page 153) A. what are obtained? (Page 154) A. Q. hexose.120 Viva—based on Textbook of Biochemistry Q. Sphingosine. Micelle and liposome. Q. N-acetyl neuraminic acid. Sphingosine. On hydrolysis of sphingomyelin. Q. Sphingomyelinase. Cerebroside contains what? A. Q. fatty acid. phosphoric acid. Beta glucosidase. will give rise to what? (Page 154) A. Niemann-Pick disease is due to the deficiency of what? (Page 157) A. fatty acid. Name some lipid storage diseases. Sphingosine.
Lipids-V 121 Q. Ganglioside. What is accumulated in Niemann-Pick disease? (Page 157) A. Tay Sach’s disease is due to the deficiency of what? (Page 157) A. What is accumulated in Tay Sach’s disease? (Page 157) A. Q. Q. Hexosaminidase. Sphingomyelin. .
They are pro-enzymes. but will be activated in the gastro intestinal tract. inactive at the time of secretion. Urea Q. Pepsin. Q. What are zymogens? (Page 158) A. Q.122 Viva—based on Textbook of Biochemistry Amino Acid Metabolism-I: General: Digestion. How pepsinogen is activated? (Page 158) A. tryptophan and methionine. Transamination. It hydrolyses peptide bonds formed by carboxyl groups of phenyl alanine. . tyrosine. What is the action of pepsin? (Page 158) A. Absorption. What is the enzyme mainly responsible for protein digestion in stomach? (Page 158) A. Removal of N-terminal end by gastric hydrochloric acid. Q.
Q. Q. . It hydrolyses peptide bonds formed by carboxyl groups of arginine and lysine. Activation is achieved by removing a small part of the precursor molecules. It is activated by trypsin. Pancreatic juice contains the endopeptidases trypsin. How trypsinogen is activated? (Page 159) A. Q. chymotrypsin and elastase. The activation of trypsinogen is by removal of a hexapeptide from N-terminal end by entero-kinase (enteropeptidase) present on the intestinal microvillus membranes. Acute pancreatitis results when trypsinogen is activated prematurely. What is an endopeptidase? (Page 159) A. What is its biological significance? (Page 158) A.Amino Acid Metabolism-I 123 Q. How chymotrypsinogen is activated? (Page 159) A. Q. What are important enzymes in pancreatic juice? (Page 158) A. It acts on peptide bonds inside the protein molecule. so that the protein becomes successively smaller and smaller units. How the activation is effected generally? (Page 158) A. Q. What is its clinical significance? (Page 158) A. Q. Selective proteolysis produces the catalytic site. Q. What is the action of trypsin? (Page 159) A. Zymogens prevent autodigestion of the cells.
(Page 160) Q. It is necessary for intracellular protein breakdown. Trypsin. spliting off carboxy terminal bond of the protein. What is required for absorption of amino acids? (Page 160) A. They act at one of the protein molecule. Give an example exopepdases. What is ubiquitin? (Page 160) A. it is an endopeptidase. Q. (Page 159) Q. In fasting state. Q. (Page 159) A. Q. pepsin. In the fasting state. Q. What are proteosomes? (Page 160) A. Q. liberating amino acids sequentially. Q. the muscle releases mainly alanine and glutamine of which alanine is taken up by liver and glutamine by kidneys. Intracellular proteases. Give some examples of an endopeptidase. It is secreted by cells of intestinal villi. What are exopeptidases? (Page 159) A. one at a time. A. What is carboxypeptidase? (Page 159) A. Ubiquitin tagged proteins are degraded inside the cells. What are cathepsins? A. It needs the help of glutathione. Carboxypeptidase. with the help of proteosomes.(Page 160) .124 Viva—based on Textbook of Biochemistry Q. it is a metallo-enzyme containing zinc. nitrogen is transported from muscle as what form? A.
What is transdeamination? (Page 161) A. Hence the term transdeamination. Alanine and alpha keto glutarate.Amino Acid Metabolism-I 125 Q. Transamination reaction of pyruvate with glutamate results in the production of what substances? (Page 161) A. Transamination of glutamic acid produces what? (Page 161) A. What is the clinical significance of transamination? (Page 161) A. Q. What is the co-enzyme necessary for transamination reaction? A. Transamination takes place in all the cells of the body. (Page 161) Q. the two components of the reaction are physically far away. it is the first step of amino acid breaking down pathways. Thus. Transaminases are increased in blood in liver and cardiac diseases. but physiologically they are coupled. Q. Alpha keto glutaric acid. What are the physiological significance of transamination? (Page 161) A. Pyridoxal phosphate. Q. it helps in the equalisation of quantities of amino acids. Q. It synthesises non-essential amino acids. . the amino group is transported to liver as glutamic acid which is finally oxidatively deaminated in liver.
Which amino acid is oxidatively deaminated in liver? (Page 162) A. Glutamate alpha keto glutarate + ammonia. NAD. What is the reaction catalysed by glutamate dehydrogenase? A. One from ammonia and another from aspartic acid. What is the reaction catalysed by glutamine synthetase? (Page 163) A. Carbamoyl phosphate synthetase. (Page 163) Q. Glutamine synthetase. CPS-II is required for pyrimidine synthesis. What is the key enzyme of urea synthesis? (Page 163) A. (Page 162) Q. Q. Q. Q. while CPS-II is in cytosol. Nitrogen atoms in the urea is derived from what precursors? A. CPS-I is involved in urea synthesis. (Page 162) Q. . Glutamic acid + ammonia ® glutamine. CPS-I is seen in mitochondria. this requires hydrolysis of ATP to ADP. Glutamic acid. Q. Ammonia is immediately trapped in brain by what? (Page 163) A. What are the two carbamoyl phosphate synthetases? (Page 164) A.126 Viva—based on Textbook of Biochemistry Q. What is the co-enzyme required for glutamate dehydrogenase? A.
Amino Acid Metabolism-I 127 Q. Blood urea level is markedly increased in which condition? (Page 165) A. Q. What is the normal blood urea level? (Page 165) A. Renal diseases. Q. 15-30 mg/day. What is the normal urinary excretion of urea? (Page 165) A. . 20-40 mg/dl.
which amino acids are used? (Page 167) A. Creatine. Serine. Q. Glycine. Glycine is used for synthesis of what compounds? (Page 166) A. methionine. Q. Serine. Arginine + glycine. Kidney. Hydroxy and Sulfur Containing Amino Acids Glycine. Bile salts. Threonine. Cysteine Q. Heme. arginine. Guanido acetic acid is formed from what amino acids? (Page 167) A. . For creatine synthesis. Purines. Guanido acetic acid is formed in which tissue? (Page 167) A. Alanine. Glutathione.128 Viva—based on Textbook of Biochemistry Amino Acid Metabolism-II: Simple. Q. Methionine.
Q. What are the important substances produced from serine? (Page 168) A. How creatinine is produced in the body? (Page 167) A. What is the significance of creatinine?(Page 167) A. In liver. Excretion is increased in muscle dystrophy.Amino Acid Metabolism-II 129 Q. phosphatidyl serine. Protein targeting defect. Q. What are the sources of oxalic acid in urine? (Page 168) A. Glycine. Q. Q. What is the product of transamination of alanine? (Page 169) A. Pyruvic acid. Choline is derived from what? A. Serine.selenocysteine. Ethanol amine. pyruvate. What is the cause of hyper oxaluria? (Page 168) A. Where is creatine is synthesised? A. By spontaneous degradation of creatine phosphate. Q. (Page 169) Q.cysteine. Q. (Page 167) Q. . Ascorbic acid and glycine. On decarboxylation. choline. serine will produce what? (Page 169) A.
Guanido acetic acid. and is taken up by liver. Cyanide nitroprusside test. (Page 173) . In liver alanine is transaminated to pyruvate. and detoxification of peroxidases. Nacetyl serotonin. keeping RBC membrane integrity.130 Viva—based on Textbook of Biochemistry Q. alanine is released from muscle. What is the methyl donor in transmethylation reaction? (Page 170) A. Gamma glutamyl cysteinyl glycine. What is the significance of glucose-alanine cycle? (Page 169) A. nor-epinephrine. Q. serine. During starvation. What are important substrates for transmethylation reactions? (Page 170) A. Q. Q. S-adenosyl methionine. Q. Which amino acid has two optically active (asymmetric) carbon atom? (Page 170) A. and pyruvate undergoes gluconeogenesis. What are the functions of glutathione? (Page 171) A. (Page 171) Q. carrying amino acids across membranes. Urine of a patient with homocystinuria will be positive for which test? A. What is glutathione? A. Reduction of met-hemoglobin to hemoglobin. Threonine. Q.
What are the characteristic features of homocystinuria? (Page 173) A. Methionine. What is the defective enzyme in Cystathionuria? (Page 173) A.Amino Acid Metabolism-II 131 Q. . Homocystinuria is due to abnormal metabolism of which amino acid? (Page 173) A. and thrombosis. subluxation of lens. Q. Q. Mental retardation. Cystathionine synthase. Q. Cystathionase. What is the defective enzyme in homocystinuria? (Page 173) A.
Glutamic acid. Isoleucine Q. Glutamine. What is the reaction catalysed by glutamate dehydrogenase? A. Valine. (Page 175) . Asparagine. Transamination. ammonia trapping in brain. Basic and Branched Chain Amino Acids. Which amino acid is oxidatively deaminated in liver? (Page 175) A. Alanine and alpha keto glutarate. What are the major functions of glutamic acid? (Page 175) A. Glutamate ® alpha keto glutarate + ammonia. Aspartic acid. transdeamination. Q.132 Viva—based on Textbook of Biochemistry Amino Acid Metabolism-III: Acidic. and production of gamma amino butyric acid. Q. Glutamic acid. Nitric Oxide. Transamination reaction of pyruvate with glutamate results in the production of what substances? (Page 175) A. Lysine. Q. Leucine.
Excretion of ammonia in kidney tubules. Which will give rise to an inhibitory neurotransmitter? (Page 175) A. Q.Amino Acid Metabolism-III 133 Q. Which is produced by decarboxylation of glutamic acid. Decarboxylation of glutamic acid will give rise to what? A. this requires hydrolysis of ATP to ADP. Q. What is the co-enzyme required for glutamate dehydrogenase? A. What is GABA? A. Glutamine synthetase. Glutamic acid. Glutaminase enzyme is used for what purpose? (Page 175) A. Glutamic acid + ammonia ® glutamine. (Page 175) Q. It is an inhibitory neurotransmitter. Gamma amino butyric acid. Q. Glutamine ® glutamic acid + ammonia. Q. What is the reaction catalysed by glutamine synthetase? (Page 175) A. Q. Q. NAD. Ammonia is immediately trapped in brain by what? (Page 175) A. Alpha keto glutarate. What is the reaction catalysed by glutaminase? (Page 176) A. Q. . Transamination of glutamic acid will give rise to what? A.
Alanine. . Q. Purines (1st nitrogen and 6th amino). Glutamic acid can be formed from which amino acids? (Page 175) A. What is its function? (Page 176) A. ammonia production in kidney (glutamine to glutamic acid + ammonia). Q. glutamine. Q. synthesis of purine (Nitrogen 3 and 9). glutamine. What are the functions of glutamine? (Page 176) A. Q.6). Alpha amino group of aspartic acid is incorporated into which compounds? (Page 176) A. Histidine.5. Transamination of pyruvic acid will give rise to what? (Page 175) A. Aspartic acid. proline. Aspartic acid. synthesis of guanine and cytosine (amino groups). Q. Ammonia production in kidney tubules. arginine. pyrimidines (1st nitrogen and C4. Which amino acids are required for both purine and pyrimidine synthesis? (Page 176) A. Transamination of oxaloacetic acid will give rise to what? (Page 175) A. Ammonia trapping in brain (glutamic acid + ammonia to glutamine). Enzyme catalysing the reaction asparaginase to aspartic acid + ammonia. Q.134 Viva—based on Textbook of Biochemistry Q. What is asparaginase? (Page 176) A. synthesis of pyrimidine (3rd Nitrogen). Q. and urea.
Nitric oxide synthase system needs which coenzymes? (Page 178) A. Carnitine is synthesised from which amino acid? (Page 177) A. Q. memory process in brain. NADPH. FMN. and the available glutamine is destroyed by glutaminase.Amino Acid Metabolism-III 135 Q. Q. FAD. What is its clinical application? (Page 176) A. Neuronal NOS. The leukemia cells cannot synthesis glutamine. Q. inhibitioin of adhesion of platelets. What are the iso-enzymes of nitric oxide synthase? (Page 178) A. What is the precursor of nitric oxide? (Page 178) A. keeping the normal blood pressure. What are the major functions of nitric oxide? (Page 178) A. Q. Q. leukemia cells will starve and die. Lysine is deficient in cereals. It is an anticancer drug against leukemias and lymphomas. Ornithine. Lysine. Q. Q. Lysine is deficient in which food stuffs? (Page 176) A. Vasodilatation. Which will give rise to polyamines? (Page 179) A. Arginine. inducible NOS (macrophages) and endothelial NOS. bactericidal in macrophages. tetra hydro biopterine. .
They are growth factors. (Page 180) Q. spermine and spermidine. and serotonin. Histamine. What are the functions of polyamines? (Page 179) A. Isoleucine joins in which metabolism? (Page 180) A. Q. Deficient decarboxylation of branched chain keto acids. Q. What about glutamine? Is it an amine? (Page 180) A. Polyamines are putrescine. Q. dopamine. Q. No. Valine is glucogenic. What is the defect in maple syrup urine disease? (Page 180) A. Q. . Valine enters in which metabolism? (Page 180) A. (Page 180) A. Maple syrup urine disease. Q. Name some mono amines. Isoleucine is partly glucogenic and partly ketogenic. Leucine is ketogenic. What are polyamines? (Page 179) A. their concentration is increased in cancer. Leucine enters in which metabolism?(Page 180) A. Glutamine is an amide of glutamic acid. Q.136 Viva—based on Textbook of Biochemistry Q. Branched chain keto acids are excreted in urine in what condition? A.
What is the immediate precursor of norepinephrine? (Page 182) A. thyroxine. In pheochromocytoma. tyrosine. Tryptophan. tryptophan. Tyrosine. Which amino acids are both glucogenic and ketogenic? (Page 181) A. . Q. urine contains what substance? (Page 183) A. Phenyl alanine. Melanin. What are the important substances synthesised from tyrosine? A. and isoleucine.Amino Acid Metabolism-IV 137 Amino Acid Metabolism-IV: Aromatic Amino Acids: Phenyl alanine. Dopamine. epinephrine and norepinephrine. Q. Vanillyl mandelic acid. (Page 182) Q. Histidine Q.
138 Viva—based on Textbook of Biochemistry Q. Phenyl alanine level in blood is increased in what condition? A. Phenyl ketonuria. (Page 183) Q. What is the defective enzyme in phenyl ketonuria? (Page 183) A. Phenyl alanine hydroxylase. Q. What are the co-enzymes required for phenyl alanine hydroxylase? A. NADH, NADPH, tetrahydro bioptrin. (Page 181) Q. Phenyl alanine, on transamination will give rise to what? (Page 183) A. Phenyl pyruvate. Q. What are the salient features of phenylketonuria? (Page 184) A. Mental retardation, hyperactivity, high blood phenyl alanine. Q. Phenyl pyruvic acid is excreted in urine in which condition? A. Phenyl ketonuria. (Page 184) Q. Homogentisic acid is excreted in urine in which condition? A. Alkaptonuria. (Page 184) Q. What is the defective enzyme in alkaptonuria? (Page 184) A. Homogentisic acid oxidase. Q. Ochronosis is a manifestation of which condition? (Page 184) A. Alkaptonuria.
Amino Acid Metabolism-IV
Q. What is associated manifestation of albinism? (Page 184) A. Nystagmus. Q. A person’s urine was found to turn black on standing and gave a positive Benedict’s test. He is likely to have what condition? (Page 184) A. Alkaptonuria. Q. In phenyl ketonuria, urine will be positive for what test? (Page 184) A. Ferric chloride test. Q. What is the defect in tyrosinemia type I (hepatorenal tyrosinemia)? A. Fumaryl acetoacetate hydrolase deficiency. (Page 185) Q. What is the defect in tyrosinemia type II (oculocutaneous tyrosinemia? (Page 185) A. Deficiency of tyrosine amino transferase. Q. Tryptophan is deficient in which food stuff? (Page 185) A. Maize and corn. Q. Xanthurenic acid in urine is seen in which condition? (Page 185) A. Pyridoxal deficiency. Q. What are the important substances produced from tryptophan? A. Serotonin, melatonin, niacin, alanine, and acetoacetate. (Page 186)
140 Viva—based on Textbook of Biochemistry Q. Which amino acid will give rise to a vitamin? (Page 186) A. Tryptophan. Q. Serotonin is derived from which amino acid? (Page 186) A. Tryptophan. Q. What are the characteristic features of malignant carcinoid syndrome (argentaffinoma)?(Page 186) A. Niacin deficiency, increased serotonin production, increased hydroxy indole acetic acid excretion, fluctuating hypertension. Q. Pellagra is manifested in which conditions? (Page 186) A. Niacin deficiency, pyridoxal deficiency, tryptophan deficiency, and carcinoid syndrome. Q. What is Hartnup’s disease? (Page 188) A. Absorption of aromatic amino acids from intestine as well as reabsorption from renal tubules are defective. So tryptophan deficiency, and pellagralike symptoms are seen. Q. Tryptophan is excreted in large quantities in which condition? A. Hartnup’s disease. (Page 188) Q. In Hartnup’s disease, which test will give a positive test? (Page 188) A. Obermeyer test will be positive in urine.
Amino Acid Metabolism-IV
Q. Indican in urine is tested by what method? (Page 188) A. Obermeyer test. Q. What is indican? A. Putrefaction product of tryptophan. (Page 187)
Q. What is the amino acid which has maximum buffering capacity at physiological pH? (Page 188) A. Histidine. Q. What is the decarboxylation product of histidine? (Page 188) A. Histamine. Q. Which is the vasodialator produced from histidine? (Page 188) A. Histamine. Q. What is the clinical significance of histamine? (Page 188) A. It is a powerful vasodilator and mediator of anaphylaxis. Q. What is Figlu excretion test? (Page 189) A. In folic acid deficiency, there is a block in histidine metabolism, and figlu is excreted in large quantities in urine. Q. What is figlu? (Page 189) A. Formimino glutamic acid, it is a product of histidine metabolism.
142 Viva—based on Textbook of Biochemistry
Amino Acid Metabolism-V:
Inter-relations of amino acid metabolisms, One carbon metabolism, Amino acidurias
Q. Tetra hydro folic acid is used for what purpose? (Page 190) A. It is the carrier of one carbon compounds. Q. Name one carbon compounds? (Page 190) A. Formyl, formimino, methenyl, hydroxymethyl, methylene, and methyl. Q. Which are the donors to one carbon pool? (Page 191) A. Serine, choline, glycine, tryptophan, histidine. Q. One carbon units are used for synthesis of what? (Page 191) A. C2 of purine, C8 of purine, serine, dTMP, choline, creatine, epinephrine.
Phenyl ketonuria. Deficiency of branched chain keto acid decarboxylase. Q.Amino Acid Metabolism-V Citric Acid Cycle 143 143 Q. maple syrup urine disease. tyrosine. homocystinuria. What are important aminoacidurias which cause mental retardation? (Page 192) A. What is the defect in alkaptonuria? (Page 192) A. What are partially ketogenic and partially glucogenic amino acids? A. Deficiency of cystathionase. What is the defect in phenylketonuria? (Page 192) A. Q. Q. What is the defect in maple syrup urine disease? (Page 193) A. (Page 192) Q. Q. isoleucine. Phenyl alanine. Q. What is the defect in homocystinuria (type 1)? (Page 192) A. Deficiency of cystathionine beta synthase. Which is the purely ketogenic amino acid? (Page 192) A. tryptophan. Deficiency of phenyl alanine hydroxylase. Deficiency of homogentisic acid oxidase. . What is the defect in cystathionuria? (Page 193) A. Leucine. Q.
cholesterol synthesis. Q. Q. What are the steps in which carbon dioxide is liberated. Give examples of substrate level phosphorylation. and ketone body formation.3-bisphospho glycerate kinase. . Acetyl CoA is produced from what substrates? (Page 194) A. Q. pyruvate kinase. during the oxidation of glucose? (Page 195) A. Acetyl CoA is used for what purposes? (Page 195) A. and succinate thiokinase. 1. Pyruvate dehydrogenase.144 Viva—based on Textbook of Biochemistry Citric Acid Cycle Q. isocitrate dehydrogenase. fatty acids. Oxidation in TCA cycle. and leucine. fatty acid synthesis. Pyruvate. (Page 195) A. alpha keto glutarate dehydrogenase.
Which is the amphibolic pathway? A. How many ATPs are generated per one rotation of the citric acid cycle? (Page 197) A. (Page 197) Q. Q. and alpha keto glutarate dehydrogenase. How TCA cycle is regulated? (Page 198) A. Q. Q. What is the inhibitor of succinate dehydrogenase? (Page 197) A. (Page 197) A. 8 ATP. Succinate thiokinase. Which is the substrate level phosphorylation step in the TCA cycle? A. 38 ATP. Availability of ATP. What is the net yield of ATP from one molecule of glucose in anaerobic glycolysis? (Page 79) A.Citric Acid Cycle 145 Q. During complete oxidation. Q. What is the net yield of ATP from one molecule of glucose in aerobic glycolysis? (Page 79) A. Q. Citric acid cycle. Give examples of reactions in which NADH is generated. (Page 194) Q. 2 ATP. Pyruvate dehydrogenase. NAD+ and oxaloacetate. . Malonate. 12 ATP. isocitrate dehydrogenase. what is the net yield of ATP from one glucose molecule? (Page 79) A. Q.
Phenyl alanine. glycogen 1%. most of the glucose is utilised by which tissue? A. Brain. histidine. In normal resting state. Isoleucine. Succinyl CoA is formed from which substrates? (Page 199) A. which substances are increased in blood? (Page 201) A. Alpha keto glutaric acid is formed from which substances? (Page 199) A. arginine.146 Viva—based on Textbook of Biochemistry Q. Q. methionine. A. Q. Fat 85%. During starvation. andodd chain fatty acids. Glutamic acid. valine. Q. Aspartic acid enters the TCA cycle at which level? (Page 199) A. Arginino succinate B. Q. Ketone bodies. protein 14%. What is the approximate percentage of storage form of energy (total fuel reserve) present in a normal human body? (Page 200) A. and epinephrine. glucagon. . and proline. (Page 200) Q. Q. Fumarate is produced from which substances? (Page 199) A. Oxalo acetate.
Q.Electron Transport Chain 147 Electron Transport Chain Q. electron transport chain. . Q. Give examples of high energy compounds. GTP. 7 kCal. On hydrolysis of 1 mole of ATP to ADP. 1. acetyl CoA. In the inner mitochondrial membrane. ATP. the release of energy will be approximately how much? (Page 206) A. What are the activities taking place inside mitochondria? (Page 207) A. How is respiratory chain organised? (Page 207) A. Where is respiratory chain located? (Page 207) A. Citric acid cycle. and succinyl CoA. and beta oxidation fatty acid. Q. Q. Components are organised into four complexes. phosphoenol pyruvate. creatine phosphate. (Page 206) A.3-bis phospho glycerate.
pyruvate dehydrogenase. It inhibits translocase. Fluid matrix contains enzymes of citric acid cycle. Q. What are FAD-linked dehydrogenases? (Page 209) A. malate dehydrogenase. What is valinomycin? (Page 210) A. Q. alpha keto glutarate dehydrogenase. beta hydroxy acyl CoA dehydrogenase. What is atractylocide? (Page 210) A. . Which cytochromes contain copper? (Page 209) A. What are NAD+ linked dehydrogenases? (Page 209) A.148 Viva—based on Textbook of Biochemistry Q. Succinate dehydrogenase. Cytochrome oxidase. dissipates the proton gradient. and acyl CoA dehydrogenase. What is the function of Co-enzyme Q? (Page 208) A. It catalyses the electron transport from complex I or II to complex III. It acts as an ionophore. Cytochrome oxidase is present in which complex? (Page 209) A. Q. and inhibits ATP synthesis. Glyceraldehyde-3-phosphate dehydrogenase. Complex IV. Where are enzymes of citric acid cycle located? (Page 207) A. Q. Q. and so inhibits ATP synthesis. isocitrate dehydrogenase. Q. Q.
Which inhibits electron transport chain at site 2? (Page 211) A.Electron Transport Chain 149 Q. Q. Naphthoquinone. Q. How many ATP are produced in the oxidation of one molecule of FADH? (Page 210) A. How many ATP are produced in the oxidation of one molecule of NADH? (Page 210) A. Q. It inhibits oxidative phosphorylation. Barbiturate. Which inhibits electron transport chain at site 3? (Page 211) A. What are the salient features of ATP synthase? (Page 210) A. Three. It has two subunits. and F1 has catalytic activity. Q. Which is complex V of respiratory chain? (Page 210) A. Q. What is oligomycin? (Page 210) A. Oligomycin. ATP synthase. Two. and cyanide. Q. Carbon monoxide and cyanide. Q. . Q. Fo is a proton channel. (Page 211) A. Which inhibits electron transport chain at site 1? (Page 211) A. carbon monoxide. Name some inhibitors of oxidative phosphorylation.
Cyanide inhibits cytochrome oxidase. Which is a physiological uncoupler? (Page 211) A. Thyroxine. (Page 211) . Q.150 Viva—based on Textbook of Biochemistry Q. What is the cause for death due to cyanide poisoning? (Page 211) A. Which is the inborn error due to a mutation in NADH-Q reductase? A. Q. Leber’s hereditary neuropathy (LHON).
and damage to various tissues. hydroxyl radical. hydroperoxyl radical. Name the free radicals. Q. NADPH oxidase. lipid peroxide radical. hydrogen peroxide. Superoxide anion radical. A. singlet oxygen. Extreme reactivity. and peroxy nitrite. . What are the enzymes generating ROS in macrophages? A. What are the important characteristics of reactive oxygen species? A. and myeloperoxidase. Q.Plasma Proteins Free Radical and Anti-oxidants 151 Free Radicals and Anti-oxidants Q. generation of new ROS by chain reaction. superoxide dismutase. short life span. nitric oxide.
loss of function.152 Viva—based on Textbook of Biochemistry Q. and peptic ulcer. ROS causes what diseases? A. mutation. Vitamin C. respiratory distress syndrome. Vitamin A. and cancer. Name important anti-oxidants. membrane damage. DNA damage. . retrolental fibroplasia. cell death. Q. rheumatoid arthritis. What are the biological effects of ROS? A. Chronic inflammation. glutathione reductase. acute inflammations. mitochondrial damage. and catalase. Q. A. Alpha tocopherol (Vitamin E). Q. reperfusion injury. bronchopulmonary dysplasia. and beta carotene. What are the free radical scavinging enzymes? A. glutathione peroxidase. atherosclerosis. Superoxide dismutase. lipid peroxidation. cataract. Protein damage.
Q. and so it is not safe to give salicylate to infants having hemolytic disease. and nephrotic syndrome. Cirrhosis liver. salicylate. Q. malnutrition. Q. bilirubin. What is normal serum albumin level?(Page 216) A. Q. albumin carries what substances? (Page 217) A. In blood. What is the normal value of total proteins in serum? (Page 216) A. 6-8 g/100 ml. What is the clinical application of albumin carrying bilirubin? (Page 217) A. Free fatty acids.Plasma Proteins 153 Plasma Proteins Q. 3.5-5 mg/dl. and calcium. Bilirubin and salicylate compete for binding to albumin. . Edema due to hypoproteinemia is seen in which conditions? (Page 217) A.
Albumin is synthesised in which organ? (Page 217) A. ceruloplasmin. Name acute phase proteins. and ceruloplasmin. chronic infections. (Page 219) A. Liver. Q. transferrin (Iron). It maintains colloidal osmotic pressure of plasma. . Where is gamma globulins synthesised? (Page 217) A. Polymorphism is exhibited by which proteins? (Page 218) A. lymph nodes). and it transports non-esterified fatty acid and bilirubin. and hemopexin (free heme). haptoglobin (hemoglobin). Q.154 Viva—based on Textbook of Biochemistry Q. Haptoglobin. Q. transferrin. Transthyretin (thyroid hormones). Q. and multiple myeloma. By reticulo endothelial system (Spleen. C-reactive protein. Name some transport proteins. nephrotic syndrome. What are the functions of albumin? (Page 217) A. (Page 218) A. Albumin globulin ratio is reversed in which conditions? (Page 218) A. thyroxine binding globulin. Q. Q. and haptoglobin. Cirrhosis. transcortin (cortisol). retinol binding protein.
Free heme. and thrombocytopenia . Albumin. Ceruloplasmin level in blood is decreased in Wilson’s hepatolenticular degeneration. males are affected. It is an acute phase protein. How hemophilia is manifested? (Page 222) A. Hemorrhage tendency is seen in which conditions? (Page 222) A. (Page 220) Q. What is ceruloplasmin? (Page 219) A. It is a copper containing enzyme (ferroxidase) seen in blood. Q. Q. Q. Vitamin K deficiency. Hemophilia. females are carriers. How hemophilia is transmitted? (Page 222) A. Q. Non-stopping hemorrhage after minor injuries. Q. What is the clinical manifestation of Alpha-1anti-trypsin deficiency? (Page 219) A. What is the clinical significance of ceruloplasmin? (Page 219) A.Plasma Proteins 155 Q. What is the carrier protein of copper? (Page 219) A. Emphysema and chronic lung infections. Hemopexin carries what? A. Q. It is inherited as an x-linked recessive trait.
Variable region. Immunoglobulin G.156 Viva—based on Textbook of Biochemistry Immunochemistry Q. What is the basic structure of an immunoglobulin? (Page 225) A. How immunoglobulins are classified? (Page 225) A. Q. Q. The antigen binding capacity of immunoglobulin resides at which region of immunoglobulin? (Page 225) A. Q. IgM. What is primary response antibody? (Page 226) A. IgG. Two heavy chains and two light chains connected by disulphide linkages. What is the secondary response antibody? (Page 226) A. Q. IgD and IgE. IgA. Immunoglobulin M. .
By somatic recombination.Heme Synthesis and Breakdown Immunochemistry 157 Q. How antibody diversity is produced?(Page 230) A. and leading to mast cell degranulation. Q. IgE attach on mast cells. It is the light chains of immunoglobulins. caused by monoclonal antibodies secreted by malignant plasma cells. Q. They mediate anaphylactic reaction. Q. It is seen in urine of 20% cases of multiple myeloma. . Q. Q. when antigen is introduced. Which antibody is seen in body secretions? (Page 227) A. excreted in urine. antigen antibody reaction occurs. What is the clinical importance of immunoglobulin E? (Page 227) A. A narrow peak in gamma globulin. Immunoglobulin A. What is the cause of anaphylactic reaction? (Page 227) A. It is precipitated when heated between 45 and 60 degrees. What is Bence Jones protein? (Page 228) A. Q. What is the test done to detect Bence Jones protein? (Page 228) A. What is M band? (Page 228) A.
It depends on vitamin C. Hydroxylation of proline and lysine needs what? (Page 233) A. Poor hydroxylation. Q. About 1% residues are proline and hydroxy proline. It has triple stranded quarter staggered arrangement. What is the structural arrangement of collagen? (Page 233) A. (Page 233) Q.158 Viva—based on Textbook of Biochemistry Specialised Proteins: Collagen. defective collagen and scurvy. Q. and hydrolysis of pro-collagen. . What are the post-translational modifications taking place in collagen? A. In ascorbic acid deficiency. what happens? (Page 233) A. Myosin Q. One-third residues are glycine. Hydroxylation of proline and lysine residues.
Q. Osteogenesis imperfecta. Q. So. It is called desmosine. dermatoparaxis. Q. It binds calcium. Q. It can bind actin to form actomyosin. Lysyl oxidase. What are inherited disorders leading to defective collagen formation? A. Ehlers-Danlos syndrome. ATPase inhibitory element. Q. It is formed between lysine and hydroxy lysine residues. What is the clinical significance of Troponin-T ? (Page 237) A. It is a specialised protein seen in muscle. Cross links in collagen are formed by what? (Page 234) A. What is the function of Troponin-I ? (Page 237) A. What is myosin? (Page 236) A. . Its serum level is increased in myocardial infarction. Q. What is the enzyme for cross linkage formation? (Page 234) A. homocystinuria. Q. It has ATPase activity. and marfan’s syndrome. What is the function of Troponin-C ? (Page 237) A. leading to defective collagen. What is its clinical application? (Page 234) A. in copper deficiency lysine cross-link formation is deficient.Specialised Proteins: Collagen Myosin Heme Synthesis and Breakdown 159 Q. (Page 234) Q. What is its biological function? (Page 236) A. Lysyl oxidase contains copper.
Q. Heme is synthesised from what substances? (Page 241) A. Which enzyme is inhibited by lead? (Page 241) A. vinyl. Alpha carbon of glycine. It is synthesised from glycine and succinyl CoA. ALA dehydratase and ferrochelatase. Methyl. Methenyl bridge of protoporphyrin is derived from what? (Page 241) A. What is the chemical structure of heme? (Page 240) A. Q. Q. . What is the rate limiting enzyme of heme synthesis? (Page 241) A.160 Viva—based on Textbook of Biochemistry Heme Synthesis and Breakdown Q. Q. and propionyl groups. It is ferro protoporphyrin. What are the substituent groups of heme? (Page 240) A. Q. ALA synthase.
Heme Synthesis and Breakdown
Q. How is heme synthesis regulated? (Page 242) A. ALA synthase is repressed by heme, and ALA synthase is allosterically inhibited by hematin. Q. What is the action of barbiturates on heme synthesis? (Page 242) A. Barbiturates will induce heme synthesis. Q. What is the treatment for acute intermittent porphyria? (Page 243) A. High carbohydrate diet, and stoppage of barbiturates. Q. What is the defect in acute intermittent porphyria? (Page 243) A. PBG-deaminase. Q. How porphyrins are detected? (Page 243) A. They show fluorescence under ultra violet light. Q. In acute intermittent porphyria, urine contains what? (Page 243) A. ALA and PBG. Q. Lead poisoning results in elevated levels of what? (Page 244) A. Delta amino levulinic acid. Q. Degradation of heme needs which enzyme? (Page 245) A. Heme oxygenase system, with NADPH. Q. Degradation of heme to bilirubin releases what gas? (Page 245) A. Carbon monoxide.
162 Viva—based on Textbook of Biochemistry Q. Heme is converted to bilirubin in which site? (Page 245) A. Microsomes of reticulo-endothelial cells. Q. Bilirubin in blood is carried by what?(Page 245) A. Albumin. Q. How it is made water soluble? (Page 245) A. By conjugation with glucuronic acid. Q. Where is the conjugation taking place? (Page 245) A. In liver. Q. What is the enzyme? A. UDP-glucuronyl transferase. (Page 245)
Q. What is the normal level of plasma bilirubin? (Page 246) A. 0.2-0.8 mg/dl. Q. What is the normal level of conjugated bilirubin in plasma? (Page 246) A. Less than 0.2 mg /dl. Q. What is latent jaundice? (Page 246) A. When plasma bilirubin is between 1 to 2 mg/dl. Q. What is jaundice? (Page 246) A. When plasma bilirubin is more than 2 mg/dl, it diffuses into tissues, causing yellowish discolouration of tissues. Q. Enterohepatic circulation is seen in which substances? (Page 246) A. Urobilinogen and bile salts.
Heme Synthesis and Breakdown
Q. What is the defect in Gilbert’s disease? (Page 247) A. Uptake of bilirubin by the liver is defective. Q. What is the defect in Criggler-Najjar syndrome? (Page 247) A. Defect in conjugation of bilirubin due to deficiency of UDP glucuronyl transferase. Q. Conjugated hyperbilirubinemia is seen in which condition? (Page 247) A. Dubin Johnson’s syndrome. Q. Bilirubin in serum is estimated by what test? (Page 247) A. Van den Bergh reaction. Q. What is Direct van den Bergh’s reaction? (Page 247) A. The colour is developed immediately when blood is added. Q. What is your inference, when direct test is positive? (Page 247) A. Blood contains conjugated bilirubin, it is water soluble. Q. What is indirect van den Bergh’s test?(Page 247) A. When blood is added to the solution, there is no colour, but when alcohol is added, colour is developed. Q. What is the reason for this type of reaction? (Page 247) A. Bilirubin is soluble in alcohol, and alcohol extract gives the reaction.
164 Viva—based on Textbook of Biochemistry Q. What is kernicterus? (Page 248) A. In young children, when plasma bilirubin is more than 20 mg/dl, it diffuses into brain, causing permanent damage to brain cells. Q. In obstructive jaundice, what is seen in blood? (Page 248) A. Conjugated bilirubin in excess quantity. Q. Bile salts and bile pigments are excreted in urine in which condition? A. Obstructive jaundice. (Page 248) Q. Increased urobilinogen in urine is seen in which conditions? (Page 248) A. Congenital spherocytosis, mismatched transfusion, Rh incompatibility, auto-immune hemolysis, and glucose-6-phosphate dehydrogenase deficiency.
Q. What are the salient structural features of hemoglobin molecule? A. Hb has four subunits, two alpha and two beta units. It contains four iron atoms. Q. How many molecules of oxygen can bind with hemoglobin? A. Hb can bind four molecules of oxygen.(Page 249) Q. 100 ml of blood can carry how much oxygen? (Page 250) A. 20 ml. Q. What is Bohr effect? (Page 251) A. The influence of pH and pCO2 to facilitate oxygenation of Hb in the lungs and deoxygenation at the tissues is known as the Bohr effect. Q. What is chloride shift? (Page 251) A. When CO2 is taken up, chloride ions from the plasma would enter. This is called chloride shift or Hamburger effect.
Q. HbF is alkali resistant. Q. Dissolved form. HbF is seen in foetal circulation. Oxygen affinity is more for HbF than HbA. isohydric transport. What are the forms in which carbon dioxide is transported? (Page 251) A.3-BPG level. Q. The H+ ions are buffered by the deoxy-Hb. How this is effected? (Page 251) A. Q. What is the physiological significance of HbF? (Page 252) A.166 Viva—based on Textbook of Biochemistry Q. HbF moves slower than HbA on electrophoresis. There is minimum change in pH during the transport. Which will decrease the affinity of hemoglobin for oxygen? A. What is the structural difference between HbA and HbF? A.(Page 252) Q. What are the laboratory tests to identify HbF? (Page 252) A. and carbamino hemoglobin. . Hemoglobin carries how much CO2? (Page 251) A. but HbF has two alpha and two gamma chains. Q. Seventy five percent as isohydric transport and 15% as carbamino hemoglobin. (Page 252) Q. 2. HbA has two alpha and two beta chains. What is isohydric transport of carbon dioxide? (Page 251) A.
The glutamic acid in the 6th position of beta chain of HbA is changed to valine in HbS. Q. presence of HbM.Haemoglobins 167 Q. Drabkin’s reagent. Q. What is the treatment for carbon monoxide poison? (Page 253) A. Q. What is the clinical significance of HbF? (Page 252) A. Hyperbaric oxygen. What is the defect of met-hemoglobin? (Page 253) A. Hb has more affinity to carbon monoxide than oxygen. Q. What is hemoglobin S? (Page 254) A. GPD deficiency. to convert Hb to cyanmethemoglobin. What is met-hemoglobin? (Page 253) A. It cannot release oxygen in tissues. What is the reagent used for colourimetric estimation of hemoglobin? (Page 254) A. . Hemoglobin in which iron is in ferric state. Q. It is seen in adults in hemoglobinopathies and thalassemias. Why carbon monoxide becomes a poison? (Page 253) A. Q. Q. Met-hemoglobin is found in which conditions? (Page 253) A. Ingestion of nitrites.
Q. the other is abnormal. Heterozygous (AS) condition. Solubility of deoxy HbS is lower than deoxy HbA. at higher altitudes. Q. What is sickle cell trait? A.168 Viva—based on Textbook of Biochemistry Q. But. and half abnormal. leading to sickle shape of RBC. Sickle cell trait persons will not have any disease manifestations. so HbS is precipitated intracellularly. What is its clinical significance? A. Chronic lung disorders may also produce hypoxia-induced sickling in HbS trait. hypoxia may cause manifestation of the disease. What is the cause for sickle cell anemia? A. How HbS is identified? A. Q. usually. . HbS is slower moving on electrophoresis than HbA. so half of Hb molecules are normal. one allele is normal.
What is the major function of Vitamin A? (Page 260) A. then isomerised to cis-retinol and then to cis retinal.Vitamin-I 169 Vitamin-I: Fat Soluble Vitamins: A. where it is made to trans-retinol. Alcohol dehydrogenase and retinol isomerase. Q. Photo-isomerisation of 11-cis retinal to all transretinal. What is the pro-Vitamin for Vitamin A? (Page 259) A. What causes the nerve impulse in retina? (Page 260) A. What are the enzymes required for this regeneration? (Page 261) A. . Q. In vision. E and K Q. Trans-retinal is taken to liver. How is all trans-retinal regenerated? (Page 261) A. Beta carotene present in plants. Q. as the Wald’s visual cycle. D. Q.
Q.25-dihydroxy cholecalciferol (DHCC). and anti-oxidant role. From 7-dehydro cholesterol in the malpighian layer of epidermis. green leafy vegetables. Cholecalciferol from skin reaches liver. How cholecalciferol is synthesised? (Page 263) A. There it is hydroxylated to form 25-hydroxy cholecalciferol (25-HCC). Vitamin A. papaya. Carrot. Q. Nyctalopia is due to the deficiency of which Vitamin? (Page 262) A. What are other minor biological roles of Vitamin A? (Page 262) A. reproduction. Q. xerophthalmia. where further hydroxylation takes place to form 1. . and keratinisation of epithelium. Normal maintenance of epithelium and skin. glycoprotein synthesis. It then reaches kidney.170 Viva—based on Textbook of Biochemistry Q. What is the daily requirement of Vitamin A? (Page 263) A. Night blindness. 750 to 1000 microgram. Q. mangoes. by the action of ultra violet rays. keratomalacia. What are the deficiency manifestations of Vitamin A? (Page 262) A. How Vitamin D is activated? (Page 264) A. What are the sources of Vitamin A? (Page 262) A. cell differentiation. Q. Q. and fish liver oil.
In renal disease. How is Vitamin D deficiency manifested? (Page 265) A. or active Vitamin D. and underexposure to sunlight. Hydroxylation and activation of Vitamin is taking place in kidney. and it also increases mineralisation of bone. Q. Vitamin D. What are the causes of rickets? (Page 265) A. oral doses of Vitamin D may not be effective. Q. It increases absorption of calcium from intestine. Q. Rickets in children and osteomalacia in adults. contains three hydroxyl groups at 1. 1. Which Vitamin acts as a pro-hormone? (Page 264) A. Q. why? (Page 265) A. The hormone-receptor complex interacts with DNA and causes transcription of specific genes that code for calbindin. liver diseases. Due to the increased availability of calcium binding protein. .Vitamin-I 171 Q. So it is called calcitriol. What is the function of Vitamin D? (Page 264) A. 3 and 25 positions. Chronic renal failure. What is calcitriol? (Page 264) A.25-dihydroxy cholecalciferol. How Vitamin D increases absorption of calcium? (Page 264) A. Q. Q. the absorption of calcium is increased. Calcitriol binds to a cytoplasmic receptor.
5-10 microgram. and palm oil. sunflower oil. safflower oil. 15 mg or 33 international units. What is the normal daily requirement of Vitamin E? (Page 266) A.172 Viva—based on Textbook of Biochemistry Q. (Page 266) Q. cotton seed oil. What is the chemical nature of Vitamin E? (Page 265) A. What is the source of Vitamin E? (Page 266) A. Vegetable oils are rich sources of Vitamin E. Alpha tocopherol. What is the daily requirement of Vitamin D? (Page 265) A. What is the relationship of selenium with Vitamin E? (Page 266) A. Q. Q. What is menadione? (Page 266) A. Anti-oxidant. . What is the function of Vitamin K? (Page 267) A. Q. It is synthetic water soluble Vitamin K. Naphthoquinone derivative. widely used in clinical practice. Q. Q. What is the function of Vitamin E ? A. Q.g. wheat germ oil. Gamma carboxylation of clotting factors such as prothrombin. Q. e. What is the chemical nature of Vitamin K? (Page 266) A. They act synergistically as anti-oxidants.
and administration of dicoumarol. Excess dicoumarol will produce what?(Page 267) A. Dicoumarol. . antibiotic therapy. Vitamin K. Q. So. Q. To prevent intravascular thrombosis. It competitively inhibits Vitamin K epoxide reductase.Vitamin-I 173 Q. What is the mechanism of action of dicoumarol? (Page 267) A. Q. Q. dicoumarol is used for what purpose? (Page 267) A. Which substance will inhibit Vitamin K? (Page 267) A. Obstructive jaundice. Vitamin C. Bleeding tendency. and platelets. Bleeding tendency is common in the deficiency of which? (Page 267) A. Excess dose of Vitamin K in neonates may lead to which condition? A. Q. Hemolysis and jaundice. (Page 267) Q. Deficiency of Vitamin K can occur in which conditions? (Page 267) A.
Transketolase. Aleurone layer of cereals (food grains) is a rich source of thiamine. Q. and alpha keto glutarate dehydrogenase. Q. Increased pyruvic acid level and increased transketolase activity. Whole wheat flour and unpolished rice and yeast are very good sources. Thiamine pyrophosphate. Which Vitamin is required for oxidative decarboxylation? (Page 268) A. In thiamine deficiency. . What is the source of thiamine? (Page 268) A. what alterations are seen in blood ? (Page 269) A. Q. Thiamine pyrophosphate is required for which reactions ? (Page 268) A.174 Viva—based on Textbook of Biochemistry Vitamin-II: Water soluble vitamins Q. pyruvate dehydrogenase.
cheilosis. Wernick’s syndrome. Vitamin B1. angular stomatits. Q.Vitamin-II 175 Q. acyl CoA dehydrogenase. Beberi is due to the deficiency of which Vitamin? (Page 269) A. (Page 269) Q. Q. What is the daily requirement of Vitamin B1 (thiamine) ? (Page 269) A. (Page 269) Q. Chronic alcoholism may lead to the deficiency of which Vitamin? A. and polyneuritis. FMN and FAD dependent enzymes. Glossitis. 1 to 1. Succinate dehydrogenase. What are the FAD dependent enzymes? (Page 270) A. and alpha ketoglutarate dehydrogenase. Beriberi. Thiamine. xanthine oxidase.5 milligram. glutathione reductase. . Q. Wernicke’s encephalopathy is due to the deficiency of which Vitamin? A. Q. Q. and circumcorneal vascularisation. Vitamin B1. glycine cleavage system. What are the clinical manifestations of thiamine deficiency? (Page 269) A. What is the co-enzyme function of riboflavin ? (Page 269) A. pyruvate dehydrogenase. What are the manifestations of riboflavin deficiency? (Page 270) A.
What is the co-enzyme function of niacin? (Page 271) A. What is the daily requirement of riboflavin? (Page 270) A.176 Viva—based on Textbook of Biochemistry Q. egg. Q. . beta hydroxy acyl CoA dehydrogenase. Name some important NAD dependent enzymes. Q. alpha. Niacin. Glucose-6-phosphate dehydrogenase.5 mg per day. Q. Which Vitamin is synthesised in the body? (Page 271) A. Rich sources are liver. (Page 271) A. 6-phospho gluconate dehydrogenase. and phenylalanine hydroxylase. (Page 271) A. and milk. Q. glyceraldehyde-3phosphate dehydrogenase. What are the important NADPH utilising reactions? (Page 271) A. beta unsaturated ACP dehydrogenase. Lactate dehydrogenase. dried yeast. malic enzyme. NAD and NADP. Beta keto acyl ACP dehydrogenase. Q. and mitochondrial isocitrate dehydrogenase. met-hemoglobin reductase. dihydrofolate reductase. and cytoplasmic isocitrate dehydrogenase. Q. HMGCoA reductase. 1. pyruvate dehydrogenase. Name the NADPH generating reactions. What is the dietary sources of riboflavin? (Page 270) A.
D. hartnup disease. Natural sources of niacin are dried yeast. About 60 mg of tryptophan will yield 1 mg of niacin. Tryptophan. peanut. What is the precursor of niacin? A. niacin deficiency. (Page 271) (Page 271) Q. Which conditions will lead to symptoms of pellagra? (Page 272) A. Q. and carcinoid syndrome. Q. About half of the requirement is met by the conversion of tryptophan to niacin. diarrhea. rice polishing. What is the daily requirement of niacin? (Page 272) A. Niacin. low tryptophan content in diet. About 60 mg of tryptophan will yield 1 mg of niacin. Tryptophan is deficient in which food stuff? (Page 272) A. The R. . Pellagra is seen in the deficiency of which Vitamin? (Page 271) A. liver. meat and fish. What are the features of pellagra ? A. Q. Tryptophan will give rise to how much niacin? (Page 272) A. Q. Maize and corn. Q. Dermatitis. legumes. What is the dietary sources of niacin?(Page 272) A. Q. Isoniazid therapy.A is 20 mg/day. and dementia.Vitamin-II 177 Q. whole cereals.
pellagra. Glutamate to GABA (gamma aminobutyric acid). (Page 273) A. decarboxylation of amino acids.178 Viva—based on Textbook of Biochemistry Q. What are the manifestations of pyridoxal deficiency? (Page 273) A. 5-hydroxy tryptophan to serotonin. Transamination reaction requires which Vitamin? (Page 272) A. peripheral neuritis. ALA synthase. (Page 272) A. and serine to ethanol amine. histidine to histamine. Infantile convulsions. Pyridoxal deficiency. cysteine to taurine. Q. Q. Pyridoxal phosphate is required for what reactions? (Page 272) A. Q. Xanthurenic acid in urine is seen in the deficiency of which Vitamin? A. Q. Give some examples of decarboxylation reactions. Give an example of transamination reaction. Pyridoxal phosphate. Alanine transaminase (ALT) will catalyse the reaction. Transamination reactions. (Page 273) Q. Blood level of ALT is increased in liver diseases. alanine to pyruvate. What is its clinical significance? A. Q. glycogen phosphorylase. AST is increased in myocardial infarction. . and anemia.
(Page 273) Q. and it is an inhibitory neurotransmitter. so B6 deficiency leads to demyelination of nerves and consequent peripheral neuritis. . one of the enzymes of this pathway is PLP dependent. What is the reason for infantile convulsions in pyridoxal deficiency? A. Q. (Page 273) Q.Vitamin-II 179 Q. PLP deficiency in turn leads to niacin deficiency which is manifested as pellagra. What is the reason for anemia in pyridoxal deficiency? (Page 273) A. absence of which leads to hyper-excitation and convulsions. PLP is required for ALA synthase. So B6 deficiency in turn leads to niacin deficiency which is manifested as pellagra. Since niacin is produced from tryptophan. Can you give an exmple of one Vitamin deficiency leading to another Vitamin deficiency? (Page 273) A. What is the reason for peripheral neuritis in pyridoxal deficiency? A. PLP is involved in the synthesis of sphingolipids. Pyridoxal phosphate is required for the formation of GABA. What is the reason for pellagra-like disease in pyridoxal deficiency? A. (Page 273) Q. In adults hypochromic microcytic anemia may occur due to the inhibition of heme biosynthesis.
180 Viva—based on Textbook of Biochemistry Q. penicillamine and oral contraceptives act as B6 antagonists. fatty acid. Q. Deficiency of pantothenic acid leads to what? (Page 274) A. Burning foot syndrome. What are the donors for acetyl CoA pool? (Page 275) A. milk. which inactivates PLP. Q. Rich sources are yeast. cereals. cycloserine. Q. Q. rice polishing. meat. Oxidation of pyruvic acid and activation of acyl groups. Ethanol in the body is converted to acetaldehyde. Q. legumes (pulses). Q. What is the function of CoA? (Page 274) A. wheat germs. Isonicotinic acid hydrazide (INH) (isoniazid). egg. Co-enzyme A. What are the dietary sources of pyridoxal? (Page 274) A. Pyruvate. What is the co-enzyme form of pantothenic acid? (Page 274) A. What is the daily requirement of pyridoxal phosphate? (Page 274) A. fish and green leafy vegetables. 1 to 2 mg/day. and amino acids. . What are the drugs which cause pyridoxal deficiency? (Page 274) A.
What is the chemical nature of folic acid? (Page 276) A. Avidin. Carboxylation reactions. What is the antagonist for biotin? A. What is PABA? A. Succinyl CoA is used for what purposes? (Page 275) A. Q. and ketone body formation. Q. Q. (Page 276) Q. Oxidation in TCA cycle. Oxidation in TCA cycle.Vitamin-II 181 Q. Acetyl CoA carboxylase. cholesterol synthesis. and activation of acetoacetate. Para amino benzoic acid. Q. (Page 275) A. steroid synthesis. (Page 276) . Name some reactions dependent on biotin. Acetyl CoA is used for what purposes? (Page 275) A. propionyl CoA carboxylase. What is its use in laboratory? (Page 276) A. fatty acid synthesis. Q. heme synthesis. (Page 275) Q. Pteroyl glutamic acid (pteridine + PABA + glutamic acid). Biotin-avidin reaction is used in immunosorbent assays. What is the function of biotin? A. and pyruvate carboxylase.
What are the other minor effects of folic acid? (Page 277) A. Q.182 Viva—based on Textbook of Biochemistry Q. Folic acid is beneficial in prevention of cancer. Pregnancy. and therefore helps in preventing heart diseases. Tetrahydro folic acid is the carrier of one carbon units. What is the major manifestation of folic acid deficiency? A. hemolytic anemias. Folic acid deficiency during pregnancy may lead to neural tube defects in the fetus. Macrocytic anemia. Tetrahydro folic acid. Folic acid deficiency in pregnancy is associated with what? (Page 277) A. Q. celiac disease). and dietary deficiency. (Page 277) Q. Folic acid prevents birth defects (fetal malformations such as spina bifida). What are the causes of folate deficiency? (Page 277) A. Q. What is the main function of folic acid? (Page 276) A. phenobarbitone). . defective absorption (sprue. Q. dilantin. phenytoin. anticonvulsant drugs (hydantoin. Folic acid is also useful to reduce the level of homo-cysteine in blood. What is the co-enzyme form of folic acid? (Page 276) A.
What is the mechanism of action of sulphonamides? (Page 278) A. Yeast. (5) Homocysteine level in blood is increased Q. They have structural similarity with PABA. What is mechanism of action of methotrexate? (Page 278) A. especially after histidine load. (3) AICAR excretion in urine. liver. (1) Normal folic acid level in serum is decreased. Methotrexate. . It inhibits folate reductase. (4) Peripheral blood picture shows macrocytic anemia. trimethoprim. It is bactericidal agent. and is a powerful anticancer drug. In pregnancy the requirement is increased to 400 mg/day. What are the sources of folic acid? (Page 278) A. cereals. What are the laboratory findings in folic acid deficiency? (Page 278) A. The RDA of free folate is 200 mg/day. and pulses. What are inhibitors of folic acid? (Page 278) A. It inhibits the folate reductase and so formation of THFA is reduced.Vitamin-II 183 Q. (2) FIGLU is excretion is more. Q. Q. pyrimethamine and sulphonamide. egg. What is the mechanism of action of trimethoprim? (Page 278) A. They are anti-bacterial agents. Q. Therefore they competitively inhibit the enzyme responsible for the incorporation of PABA into folic acid. Q. Q. green leafy vegetables. What is the daily requirement of folic acid? (Page 278) A.
Methyl B 12. Corrin ring. Vitamin B12. What is the storage form of Vitamin B12? (Page 279) A. a glycoprotein. It is stored in the liver cells. Cobalt. as ado-B12 form. What is the ring system present in Vitamin B 12? (Page 279) A. Q. is the specific carrier. Methyl malonyl CoA isomerase. Transcobalamin-II. Ileum. Q. . What is the metal present in Vitamin B12? (Page 279) A. Q. What is the carrier of Vitamin B12 in blood? (Page 279) A. Q. What is the co-enzyme function of Vitamin B 12? (Page 279) A. and homocysteine methyl transferase. Vitamin B12 is absorbed from where?(Page 279) A. What is the transport form of Vitamin B12? (Page 279) A. A.184 Viva—based on Textbook of Biochemistry Q. Name a water soluble Vitamin. Q. which is stored in the body. Q. (Page 279) Q. in combination with transcobalamin-I or transcorrin.
Homocysteinuria is also seen. When B12 is deficient. The production of methyl THFA is an irreversible step. What is the clinical importance of folate trap? (Page 280) A. there is non-availability of active methionine. by a Vitamin B12 dependent step. This leads to deficient formation of myelin sheaths of nerves. Q. What abnormal compound is excreted in Vitamin B12 deficiency? A. accumulation of methyl malonic acid. Q. This is called the methyl folate trap. (Page 280) . Therefore. (Page 280) Q. What is the explanation of demyelination in Vitamin B12 deficiency? A. this reaction cannot take place. Methyl malonic acid in urine. What abnormalities are seen in Vitamin B 12 deficiency? (Page 280) A. methylation of phosphatidyl ethanolamine to phosphatidyl choline is not adequate. This leads to the associated folic acid scarcity in B12 deficiency. Methyl malonic aciduria. Therefore. the only way for generation of free THFA is methyl THFA to THFA. What is folate trap? (Page 280) A.Vitamin-II 185 Q. In Vitamin B12 deficiency. breakdown of myelin sheaths and interruption in nerve transmission. Q.
leading to defective absorption of B12. It is an autoimmune disease with a strong familial background.186 Viva—based on Textbook of Biochemistry Q. Q. Antibodies are generated against intrinsic factor. In folate deficiency. there is additional neurological symptoms also. . So IF is deficient. What are the manifestations of Vitamin B12 deficiency? (Page 280) A. atrophy of gastric epithelium. What is the difference in folate deficiency and B12 deficiency? A. (Page 280) Q. What is the daily requirement of Vitamin B12? (Page 280) A. there is macrocytic anemia. Vitamin B12. Q. Megaloblastic anemia and subacute combined degeneration. What are the causes of B12 deficiency? (Page 280) A. decrease in absorption. Q. What is the cause for pernicious anemia? (Page 280) A. A patient who has undergone gastrectomy is likely to develop deficiency of which Vitamin? (Page 280) A. Nutritional B12 deficiency. and pregnancy. One to two microgram/per day. addisonian pernicious anemia. Q. and in B12 deficiency.
Which is the Vitamin totally absent in plant sources? A. Man and primates cannot synthesise ascorbic acids. What are the other functions of ascorbic acid? (Page 282) A. Parahydroxy phenyl pyruvate oxidation to homogentisic acid. Lower animals could synthesise it from glucose through glucuronic acid pathway.Vitamin-II 187 Q. (Page 281) Q. what are the abnormalities seen in urine? A. Q. Q. Q. fish. Urine may contain methyl malonic acid. reconversion of methemoglobin to hemoglobin. cystathione. What are the major functions of ascorbic acid? (Page 282) A. Q. meat. What are the sources of Vitamin B12?(Page 280) A. and adrenal steroidogenesis. In Vitamin B12 deficiency. . homocystine. L-ascorbic acid. iron absorption from the intestine. Vitamin B12. and curd. (Page 280) Q. and formimino glutamic acid. How it is synthesised? (Page 282) A. Liver. Ascorbic acid promotes collagen formation through its action on post-translational hydroxylation of proline and lysine residues. What is the chemical structure of Vitamin C? (Page 282) A.
Ascorbic acid.188 Viva—based on Textbook of Biochemistry Q. bleeding gums. . What are the important features of scurvy? (Page 283) A. What is the daily requirement of ascorbic acid? (Page 283) A. Hemorrhagic tendency. Q. Q. (Page 282) Q. Which Vitamin is required for post-translational modifications? A. bone pain. microcytic anemia. Ascorbic acid. Scurvy is due to the deficiency of which Vitamin? (Page 283) A. 75 mg per day.
. Milk. and vegetables. What is the normal level of calcium in blood? (Page 285) A. 9-11 mg /dl. intracellular messenger. Q. and oxalate. What influences absorption of calcium from intestine? (Page 284) A. egg. calcitriol. What is the function of calcium ? (Page 285) A. Vitamin D. fish. phytic acid. parathyroid hormone. What is the daily requirement of calcium? (Page 284) A. neuromuscular activity. Q. 500 mg per day. What are the sources of calcium? A. activation of enzymes.Mineral Metabolism 189 Mineral Metabolism Q. (Page 284) Q. and bone formation. Q. Coagulation.
Tetany. (Page 287) A. and urinary calculi. Calcitriol. increased absorption of calcium from intestines. Hypocalcemia results in what clinical condition? (Page 287) A. Q. aldosterone. What is the reason for tetany? A. Which will influence serum calcium level? (Page 285) A. . Q. Q. hypercalciuria. What is the important extracellular cation? (Page 289) A. Q. How parathyroid hormone regulates calcium level in blood? A. Sodium. and cortisone. What is the normal level of phosphorus in blood. 136-145 mEq/L. What are the features of hyperparathyroidism ? (Page 287) A. Hypoparathyroidism. (Page 287) Q. (Page 286) Q. calcitonin. 3-4 mg /dl. Osteoporosis. Q. Bone resorption.190 Viva—based on Textbook of Biochemistry Q. What is the normal level of sodium in blood ? (Page 289) A. Which will control the sodium level in serum? (Page 289) A. Q. ADH. and increased absorption of calcium from renal tubules. and parathyroid hormone.
Q. Which is the trace element. Potassium. Q. What are important iron containing proteins? (Page 291) A. meat. ST segment is lowered. Iron.106 mEq /L. What is the manifestation of hypokalemia? (Page 289) A. 96. What is the normal level of chloride in blood ? (Page 290) A. transferrin. Hemoglobin. xanthine oxidase. and jaggery. (Page 291) Q. Green leafy vegetables. In ECG. tryptophan pyrrolase. Q. Which will increase iron absorption from intestines? (Page 291) A. Q. What is the daily requirement of iron for a normal adult male ? A. 3. myoglobin.Mineral Metabolism 191 Q.5 to 5 mEq /L. Gastric HCl. . 10-20 milligram per day. Q. What is the normal level of potassium in blood ? (Page 289) A. deficient in milk? (Page 291) A. What is the major intracellular cation?(Page 289) A. ascrobic acid. cytochromes. and cysteine. T wave inverted. catalase. Q. and ferritin. Q. What are the dietary sources of iron ? (Page 291) A.
Iron in the intestinal lumen enters the mucosal cell in the ferrous state. This is bound to transferrin molecule present in brush border surface of intestinal cell. Q. This iron-transferrinreceptor is internalised. (Page 292) Q. How iron absorption is regulated? (Page 292) A. What is the carrier protein in iron in blood? (Page 292) A. absorption is decreased. lead and phosphates. One transferrin molecule can bind with two atoms of iron. Q. Iron metabolism is unique because homeostasis is maintained by regulation at the level of absorption and not by excretion. Iron is absorbed from which part? A. Which enzyme will help in iron carriage in blood? (Page 292) A. When iron stores in the body are depleted. Phytic acid (in cereals) oxalic acid (in leafy vegetables). When adequate quantity of iron is stored. Ferroxidase (ceruloplasmin).192 Viva—based on Textbook of Biochemistry Q. absorption is enhanced. Q. Q. Transferrin. calcium. zinc. This is referred to as “mucosal block” of regulation of absorption of iron. . Upper part of duodenum. How is iron absorbed? (Page 292) A. What are the factors which will retard iron absorption? (Page 291) A. This is then complexed with a specific receptor.
and liver. lysyl oxidae. What is the storage form of iron? A. Q. meat. cytochrome C. It is the carrier of free hemoglobin. folic acid. (Page 293) Q. Anemia is resulted in the deficiency of which substances? (Page 293) A. What are the important copper containing enzymes? (Page 294) A. Cereals. and pyridoxal phosphate. and super oxide dismutase. . Q. What is the cause for hemosiderosis? (Page 294) A. Q. Iron deficiency results in what? A. tyrosinase. What is haptoglobin? A. copper. Q. Ferritin. (Page 293) (Page 293) Q. (Page 294) Q. Excess iron is loaded as hemosiderin. and yellow colour of skin. Q. Cirrhosis of liver. What are the features of hemosiderosis? (Page 294) A. It is the carrier of free heme. diabetes mellitus. Q. What are dietary sources of copper? (Page 294) A. Ceruloplasmin.Mineral Metabolism 193 Q. What is hemopexin? A. vitamin B12. Microcytic hypochromic anemia. What is hemosiderin? (Page 293) A. Repeated transfusion of whole blood. Iron. vitamin C. cytochrome oxidase.
Name the selenium containing enzyme. It is an anti-oxidant. 150-200 microgram. Zinc is required for insulin secretion. What is the importance of selenium? (Page 298) A. Q. . amylase. Osteoporosis is the manifestation. What are the important enzymes which contain zinc? (Page 296) A. It is produced when fluoride concentration in water is more than 20 ppm. What is Fluorosis? (Page 297) A. Alkaline phosphatase. Q. carbonic anhydrase. It is ferroxidase. copper excretion is reduced. Q. What is the daily requirement of iodine? (Page 295) A. Ceruloplasmin level in blood is decreased.194 Viva—based on Textbook of Biochemistry Q. and RNA polymerase. (Page 298) A. What is ceruloplasmin? (Page 294) A. and it promotes oxidation of ferrous ion to ferric form. Q. 15-20 milligram. Q. and copper is accumulated in liver to produce cirrhosis. What are the characteristic features of Wilson’s hepatolenticular degeneration? (Page 295) A. Q. Glutathione peroxidase. What is the daily requirement of zinc? (Page 296) A. Q.
Q. What is the calorific value of carbohydrates? (Page 299) A. What is the respiratory quotient? (Page 299) A. Q. One. Nine kilocalories per gram. What is the calorific value of fats? A. It is the ratio of carbon dioxide produced to the oxygen consumed. (Page 299) . Q. How much calories are generated per gram of fat ? (Page 299) A. Q. kCal. What is the respiratory quotient of carbohydrates? (Page 299) A. Four kilocalories per gram.Energy Metabolism and Nutrition 195 Energy Metabolism and Nutrition Q.
Q. Basal metabolic rate is increased in which conditions? (Page 300) A. (Page 302) A. Q. What are the beneficial effects of dietary fibre? (Page 301) A. Q. Q. Linoleic acid. Fever. Which foodstuff has maximum specific dynamic action ? A.196 Viva—based on Textbook of Biochemistry Q. and groundnut oil. What is specific dynamic action? (Page 300) A. Name an undigestible carbohydrate. starvation. (Page 301) A. Proteins. Q. sunflower oil. Q. Grave’s disease (hyperthyroidism). and increased thyroid hormones. . Which food stuffs contain polyunsaturated fatty acids? (Page 302) A. decreased absorption of cholesterol. Increased motility of intestine. About 0. What is the respiratory quotient for a mixed diet? (Page 299) A. linolenic acid. (Page 300) Q. and arachidonic acid. cold climate. (Page 300) Q. Vegetable oils. Pectin.82. Name essential fatty acids. Increased basal metabolic rate is observed in which clinical condition? A. Increased heat production after intake of food. and increased glucose tolerance.
They should take polyunsaturated fatty acids. Q. Phenyl alanine is deficient in which food stuff? (Page 305) A. convalescence. (Page 302) Q. Q. What is the recommended daily allowance of protein of a normal adult? (Page 303) A. (Page 302) Q. Egg. (Page 303) Q. Cereals. and growth period. Methionine is deficient in which food stuff? (Page 305) A.Energy Metabolism and Nutrition 197 Q. butter. and malnutrition. 1 g/kg. What is the dietary advice for a patient with hypercholesterolemia? A. Tapioca. and pig fat. Chronic infection. Positive nitrogen balance is observed in which conditions? A. Q. Lysine is deficient in which foodstuff? (Page 305) A. ghee. old age. A patient with coronary artery disease is advised to refrain from what? A. Egg. Negative nitrogen balance is observed in which conditions? A. . What foodstuffs contain cholesterol? (Page 302) A. (Page 303) Q. Pregnancy. Q. Pulses.
(Page 307) Q. proteins and fats in which ratio? (Page 307) A. A balanced diet should have calories for carbohydrate. Supplementation by combining cereals and pulses. Hypoalbuminemia. with sedentary work? A. and loss of appetite. How all amino acids are made available in a mixed diet? A. 2000 kCal. . 306) A.198 Viva—based on Textbook of Biochemistry Q. (Page 305) Q. How much energy is required for a 60 kg person. What are the salient features of Kwashiorkor? (Page 305. 60:20:20. Q. growth retardation. lethargy. hypomagnesemia.
(Page 311) A. Q.Detoxification and Biotransformation of Xenobioticsn Acid Base Balance and pH 199 199 Detoxification and Biotransformation of Xenobiotics Q. Give an example of a substance detoxified by reduction. Acetanilide to aniline + acetate. Biochemical processes whereby noxious substances are rendered less harmful or more water soluble and easily excretable. They are compounds accidentally ingested or taken as drugs or compounds produced in the body by bacterial metabolism. What is detoxification process? (Page 310) A. What are xenobiotics? (Page 310) A. Para nitro phenol. (Page 311) A. Q. Give examples of substances detoxified by hydrolysis. Q. aspirin to salicylic acid + acetate. .
and cysteine. (Page 311) A. (Page 311) A. What is the methylating agent? A. A. glycine. Which amino acids are used for detoxification? (Page 311) A. (Page 311) Q. Q. Glutamine. glutathione. How benzoic acid is detoxified? (Page 311) A. Q.200 Viva—based on Textbook of Biochemistry Q. (Page 312) (Page 312) . phenol to phenyl sulfate. What is the sulfating agent? (Page 311) A. and indole to indoxyl sulfate. S-adenosyl methionine. Q. Q. PAPS (phospho adenosyl phospho sulfate). Give examples of substances detoxified by sulfation. Phenol to phenyl sulfate. PAPS. and glycine. Bilirubin to bilirubin glucuronide. Q. Give some examples of substances detoxified by conjugation. Benzoic acid + glycine = benzoyl glycine or hippuric acid. and benzoic acid to hippuric acid. As methyl conjugates. Give names of conjugating agents. UDP glucuronic acid. How epinephrine is excreted? A. Q.
more than 10 ?g/dl in children and more than 25 ?g/dl in adults lead to toxic manifestations. painting and printing. What is the most common environmental poison? (Page 314) A. newspapers. lead pipes. What are the occupations in which persons are prone to get lead poisoning? (Page 314) A. . Lead.Biochemical Aspects of Environmental Pollution Acid Base Balance and pH 201 Biochemical Aspects of Environmental Pollution Q. Paint. xerox copies and cigarette smoke are important contaminants. soldering. radiator repair. What are common causes of lead poisoning? (Page 314) A. Blood level of lead. Q. lead containig petrol. Q. Battery repair. What is the toxic level of lead? (Page 314) A. Q.
discolouration and blue line along the gums. What is the cause of anemia in lead poisoning? (Page 314) A. What are the manifestation of acute lead poisoning? (Page 314) A. ALA-dehydratase and ferrochelatase. What are the manifestations of chronic lead poisoning? (Page 314) A. severe anemia and kidney damage. Anemia.202 Viva—based on Textbook of Biochemistry Q. Life span of RBC is shortened. Q. Anemia enhances lead absorption. Calcium dodecyl edetate (Calcium disodium versenate). behavioral problems. abdominal colic and loss of appetite are very common. Dimercaptosuccinic acid is a better but costly antidote. If the blood level of lead is more than 70 mg/dl. penicillamine and dimercaprol (BAL) are used as antidotes. heme synthesis is blocked. stillbirth. When does acute toxicity is manifested? (Page 314) A. mental retardation. What are the antidotes for lead poisoning? (Page 314) A. In children. and premature birth. Q. neuropathy. . mania. learning disabilities. hyperexcitability and seizures are seen. Lead inhibits delta amino levulinic acid (ALA) synthase. So. lead in turn produces more anemia. Encephalopathy. acute toxicity is manifested. Q. convulsions. thus a vicious cycle is operating. Q. Miscarriage. abdominal colic.
By the ratio of salt to acid. Q. Q. (Page 320) Q. Henderson-Hasselbalch’s equation. When is the buffering capacity is more? (Page 320) A. When the absolute concentrations of salt and acid are more. Q. Q. When pK of the acid is nearer to pH. Relationship between pH and pK is given by which equation? (Page 320) A.Acid Base Balance and pH 203 Acid Base Balance and pH Q. what is the change in the hydrogen ion concentration? (Page 319) A. What determines the pH of buffer? A. . Increases by 10 times.1 M hydrochloric acid? (Page 319) A. Buffer is most effective when? (Page 320) A. What is the pH of 0. One. When pH falls by 1 unit.
lung mechanism. What are the mechanisms for maintaining the normal pH of plasma? (Page 321) A. Buffers of plasma. In the blood. Q. What is metabolic acidosis? A. and production of bicarbonate in renal tubules. and diarrhea. and kidney mechanism. Excretion of hydrogen ions in urine. . chronic renal failure. Glutaminase enzyme is used for what purpose? (Page 323) A. Q. What are the causes of metabolic acidosis? (Page 326) A. Q. For production of ammonia in kidney tubules. excretion of ammonium ions in urine. What is the alkali reserve of the body? (Page 321) A. Primary deficit of bicarbonate. What are the mechanisms by which renal regulation of acid load is achieved? (Page 323) A. which buffer is most effective? (Page 321) A. (Page 325) Q. Bicarbonate is the alkali reserve. Q.204 Viva—based on Textbook of Biochemistry Q. Bicarbonate to carbonic acid ratio is 20. Diabetic ketosis. Q. What is the ratio of bicarbonate to carbonic acid in blood? (Page 321) A. Bicarbonate buffer. Q.
(Page 326) Q. Primary excess of bicarbonate. Q. Lowered bicarbonate. What is the formula used to calculate anion gap? (Page 326) A. Bronchial asthma. and narcotic poisoning. bronchopneumonia. What is respiratory alkalosis? A. Q. Primary excess of carbonic acid. What are the causes of metabolic alkalosis? (Page 326) A. Diabetic ketoacidosis. renal tubular acidosis. What is respiratory acidosis? A. Q. (sodium + potassium) minus (chloride + bicarbonate). and ingestion of antacids. What is the cause for high anion gap acidosis? (Page 326) A. and increased anion gap. What is metabolic alkalosis? A. (Page 327) . What are the features of diabetic ketoacidosis? (Page 326) A. gastric aspiration. What are the causes of respiratory acidosis? (Page 327) A. Q. Primary deficit of carbonic acid.Acid Base Balance and pH 205 Q. chronic renal failure. (Page 326) Q. Q. elevated plasma chloride. lactic acidosis. Prolonged vomiting.
.206 Viva—based on Textbook of Biochemistry Q. What are the results of prolonged vomiting? (Page 327) A. hypochloremia. Q. Alkalosis. What is the cause for respiratory alkalosis? (Page 327) A. and hypokalemia. Hyperventillation.
and retains water in the body. What is the major intracellular cation?(Page 329) A. Q.ElectrolyteMolecular Biology I and Water Balance 207 Electrolyte and Water Balance Q. What are the diuretic drugs used? (Page 330) A. Q. Potassium. Q. What are the factors regulating fluid and electrolyte balance? A. Its secretion is stimulated when plasma osmolarity increases. angiotensin converting enzyme inhibitors. What is the major extracellular cation?(Page 329) A. and carbonic anhydrase inhibitors. . Aldosterone antagonists. Sodium. What is the function of anti diuretic hormone? (Page 330) A. Aldosterone and anti diuretic hormone. ADH decreases the urine output. (Page 330) Q.
What is the major cause for isotonic contraction of ECF? (Page 331) A. . Addison’s disease. What are the causes for hypotonic contraction of ECF? (Page 331) A. Q. Q. vomiting. (Page 331) Q. Infusion of dextrose (without saline). What are the metabolic imbalances seen in diarrhea? (Page 331) A. Small intestinal obstruction. Inappropriate secretion of ADH. Q. What is the important cause for hypertonic expansion of ECF? A. What are the causes for hypertonic contraction of ECF? (Page 331) A. What are the causes for isotonic expansion of extracellular fluid? A.208 Viva—based on Textbook of Biochemistry Q. urine with high specific gravity. Diarrhoea. and urine output reduced. Cushing’s syndrome. What is the cause for hypotonic expansion of extracellular fluid? A. (Page 331) Q. Metabolic acidosis. hypertonic contraction of ECF. Congestive cardiac failure and hyperaldosteronism. (Page 331) Q.
Q. Purines and pyrimidines. What are the bases present in nucleotides? (Page 332) A. Cytosine. (Page 332) Q. Chemistry and Metabolism Q. A. Nitrogenous base + sugar. Name the common pyrimidines. Name the common purines.Molecular Biology I 209 Molecular Biology-I: Nucleotides. and thymine. Q. Q. Q. A. Nitrogenous base + sugar + phosphate. Adenine and guanine. What is a nucleotide? (Page 332) A. (Page 332) (Page 332) . uracil. What is a nucleoside? A. What are the sugars? (Page 332) A. Ribose in RNA and deoxyribose in DNA.
and thymine. Which base is found exclusively in RNA and not in DNA? (Page 332) A. N3 of purine ring is donated by what?(Page 335) A. Uracil. N7 atoms. Q. Q. C5. Adenine. Thymine. Glutamine. C2 and C8 carbon atoms. N1 atom of purine ring is coming from what? (Page 335) A. Q. Which amino acid is required for both purine and pyrimidine synthesis? (Page 333) A. One carbon pool donates which carbon atoms of purine ring? A. Uracil. Glycine donates what part of the purine ring? (Page 335) A.210 Viva—based on Textbook of Biochemistry Q. Q. Q. Aspartic acid and glutamine. Q. cytosine. Q. Which nitrogenous base is absent in DNA? (Page 332) A. (Page 335) . C4. Which base is found exclusively in DNA and not in RNA? (Page 332) A. guanine. Aspartic acid. What are the bases present in DNA? (Page 332) A. Q.
How is de novo synthesis of purine regulated? (Page 337) A. Give a few examples of purine analogues.Molecular Biology I 211 Q. Adenine phospho ribosyl transferase (APRTase) and hypoxanthine guanine phospho ribosyl transferase (HGPRTase). 6-mercapto-purine inhibits the conversion of IMP to GMP and AMP. (Page 338) A. They act as cell cycle inhibitors and can be used as anti-cancer drugs. Cytosine arabinoside. . What is the importance of the salvage pathway? (Page 337) A. Q. 2. Amidotransferase enzyme is inhibited by AMP and GMP. Folate antagonists (Methotrexate) would affect the reactions involving one carbon group transfers. What is the key enzyme of de novo synthesis pathway of purines? (Page 337) A. What are the enzymes needed for salvage pathway of purines? (Page 337) A. What is the clinical significance of the purine analogues? (Page 338) A. Q. Q. Q. used as anti-cancer drugs. Q. The committed step in de novo synthesis is the reaction catalysed by amidotransferase (step 1). This is of special importance in tissues like RBCs and brain where the de novo pathway is not operating. 3. 4. Azaserine is a glutamine antagonist and therefore inhibits reactions involving glutamine.
Hodgkin’s lymphoma. What is the normal excretion rate of uric acid? (Page 338) A. leukemia. Gout. . Increased uric acid level is seen in which conditions? (Page 339) A. molybdenum and iron. Uric acid is sparing soluble in water. What is the speciality in this reaction?(Page 338) A. Which property of uric acid is responsible for the manifestations of gout? (Page 338) A. The daily excretion of uric acid varies from 500700 mg. As xanthine is oxidised to uric acid. pre-eclampsia. It is the enzyme for the reactions. Q. (Page 338) Q. Q. The normal blood level of uric acid ranges from 2-5 mg/dl in females and 3-7 mg/dl in males. Q. Q. and diabetic ketoacidosis. Uric acid.212 Viva—based on Textbook of Biochemistry Q. Q. hypoxanthine to xanthine and xanthine to uric acid. What is the end product of catabolism of purines in human beings? A. hydrogen peroxide (reactive oxygen species) is produced. What is xanthine oxidase? (Page 338) A. What is the normal uric acid level in blood? (Page 338) A. Xanthine oxidase is a metalloflavoprotein containing FAD.
Gout. and glutathione reductase. Severe immunodeficiency. Adenosine deaminase deficiency. Q. It is what type of inhibition? (Page 340) A. Q. HGPRTase. Q. Ribosyl amido transferase. and X-linked inheritance. It inhibits xanthine oxidase. Xanthine oxidase converts allopurinol to alloxanthine. This is a good example of ‘suicide inhibition. What are salient features of Lesch-Nyhan syndrome? (Page 340) A. Glucose-6-phosphatase. Self mutilation. Hyperuricemia is observed in which conditions? (Page 339) A. (Page 340) . Lesch Nyhan syndrome. PRPP synthetase.Molecular Biology I 213 Q. Hypouricemia can result from deficiency of which enzyme? (Page 340) A. Q. von Gierke’s disease. It is an analogue of hypoxanthine. Q. Q. How is it manifested? A. Hyperuricemia can result from defect of which enzymes? (Page 339) A. and thereby decreasing the formation of uric acid. APRTase. It is a more effective inhibitor of xanthine oxidase. What is the mechanism of action of allopurinol? (Page 340) A. hyperuricemia.
What is carbamoyl phosphate synthetase II and how is it different from type I enzyme? (Page 341) A. Carbamoyl phosphate and aspartic acid. but CPS-I is for urea synthesis. Aspartyl trans carbamoylase. CPS-II is in cytosol. Q. Orotic aciduria is a feature of deficiency of which enzymes? (Page 342) A. and ornithine transcarbamoylase. What are used for pyrimidine synthesis? (Page 340) A. Q. CPS-II is involved in pyrimidine synthesis. What is the mechanism of action of 5-fluoro uracil? (Page 342) A. . How is pyrimidine synthesis pathway regulated in mammals? A. Q. What is the mechanism of action of 6-mercpto purine? (Page 342) A. and so acts as an antimetabolite.214 Viva—based on Textbook of Biochemistry Q. It inhibits conversion of dUMP to dTTP. (Page 341) Q. OMP decarboxylase. CPS-II is inhibited by CTP. CPS II is inhibited by CTP. Q. and acts as an antimetabolite. but CPS-I is in mitochondria. What is the rate limiting step in pyrimidine synthesis? (Page 340) A. whereas CPS-I is not. It inhibits conversion of IMP to AMP. OPRTase. Q.
Methylation of dump is done by thymidylate synthase. Formation of dTMP (thymine nucleotide) requires what enzyme and co-enzymes? (Page 342) A. . using NADPH. By the reduction at the 2' carbon of the corresponding nuceloside diphosphates (NDP to dNDP). How deoxyribonucleotides are formed? (Page 342) A. urinary tract obstruction. The methyl group is donated by methylene-THFA. Megaloblastic anemia. and thioredoxin. and response to oral uridine therapy. Q. Ribonucleotide reductase. Later. THFA is regenerated by dihydrofolate reductase. What are the enzymes and co-enzymes for this reaction? (Page 342) A. NADPH. and it is a powerful anticancer agent. Methotrexate inhibits dihydrofolate reductase and thereby reduces the regeneration of THFA. Q. Q. What are the characteristic features of orotic aciduria ? (Page 342) A.Molecular Biology I 215 Q.
Acetylation. DNA wrapped around histones. (Page 345) . Pairing (hydrogen bonding) of adenine with thymine and guanine with cytosine. What is base pairing rule? (Page 344) A. Q. Purine is paired with pyrimidine A+T = G+C. Q. What are the modifications seen in histones? (Page 345) A. Right-handed double helix. What is nucleosome? A. Q. and phosphorylation. What are the important characteristics of WatsonCrick model of DNA? (Page 344) A. Hydrogen bonds between purines and pyrimidines. methylation.216 Viva—based on Textbook of Biochemistry Molecular Biology-II: DNA structure and Replication Q. each turn of helix has 10 base pairs. and DNA strands running in opposite directions (anti parallel).
each daughter cell gets an exact copy of the genetic information of the mother cell. (Page 347) Q. topo isomerase. . This forms a replication bubble. What a replisome? (Page 347) A. Five. and sensitive to digestion by DNAse. What is euchromatin? (Page 346) A. DNA polymerase. Alpha. Transcriptionally active chromatin is called euchromatin. Q. collectively called DNA replicase system or replisomes. Q. During cell division. How the exact copying is effected? (Page 346) A. It is less densely packed. over which a new complementary strand is synthesised. separating the strands in advance of the replication.Molecular Biology-III II 217 Q. and epsilon. What is meant by DNA replication? (Page 346) A. Each strand serves as a template or mould. How many DNA polymerases are there in mammalian cells? A. The base pairing rule is always maintained. This process of copying the DNA is known as DNA replication. Q. DNA replication needs the participation of more than 20 enzymes and proteins. gamma. delta. Helicases move on both directions. What is a replication bubble? (Page 348) A. beta. Q. Q. What are the enzymes required for DNA replication? (Page 347) A. and DNA ligase.
What is lagging strand? (Page 348) A. . Q. The small DNA molecules attached to its own primer RNA in the lagging strand are called okazaki fragments. What is meant by semi-discontinuous nature of replication? (Page 348) A. the replication is taking place continuously. but in the other strand replication is in small pieces. is synthesised by the RNA primase. Replication fork advances towards one side. So. In the daughter cell. This means that the template is read in the 3' to 5' direction. What is meant by semiconservative nature of replication? (Page 346) A. one strand is derived from the mother cell. in one strand. How replication starts? (Page 347) A. Q. Replication is in which direction? (Page 347) A. Polymerisation of the new strand of DNA is taking place from 5' to 3' direction. This is called semi-conservative type of DNA replication. The RNA is removed and DNA pieces are joined by ligases. What are okazaki fragments? (Page 348) A. DNA synthesis is always in the 5' to 3' direction in both strands. Q. An RNA primer. The strand which is discontinuously synthesised is referred to as the “lagging strand” and the one continuously polymerised as the “leading strand”.218 Viva—based on Textbook of Biochemistry Q. Q. while the other strand is newly synthesised. Q. about 100-200 nucleotides long.
Molecular Biology-III II 219 Q. Xeroderma pigmentosum is due to deficiency of what process? (Page 349) A. nalidix acid. and novobiocin. Which enzymes protects cellular ageing? (Page 350) A. In prokaryotes. DNA replication is inhibited by what drugs? A. and etoposide. Fanconi’s anemia. Defect in DNA repair mechanisms produce what clinical conditions? A. Q. ataxia-telangectasia. DNA replication in eukaryotes is inhibited by what drugs? (Page 350) A. Xeroderma pigmentosum. Defect in DNA repair mechanism (nucleotide excision repair). Q. Ciprofloxacine. 6-mercaptopurine. and Bloom’s syndrome. 5-fluoro uracil. (Page 350) Q. . (Page 350) Q. cytosine arabinoside. Telomerase.
What is coding strand? (Page 351) A. What are the different types of RNAP? (Page 351) A. The mRNA is a complementary copy of which strand of DNA? A. The process of making a complementary mRNA copy of DNA. What is transcription? (Page 351) A. The opposite strand of template strand.220 Viva—based on Textbook of Biochemistry Molecular Biology-III: Transcription and Translation Q. Q. . What is the enzyme necessary for the transcription? (Page 351) A. Q. Q. DNA dependent RNA polymerase or RNAP. RNAP type I or A is responsible for synthesis of rRNA while type III or C is responsible for production of tRNA. Template strand. (Page 351) Q. Coding strand has the same sequence as of the mRNA. RNAP type II or B is the enzyme synthesising mRNAs.
Q. So the mRNA makes a hairpin structure. This is transcribed. This obstructs further movement of RNA. There is also Rho Independent Termination. introns. then the RNAP enzyme dissociates from DNA. What are post-transcriptional modifications? (Page 353) A. Q. It takes place in the 5' to 3' direction. RNAP II is inhibited by alpha amanitin. Q. It is located at -25 to -30 position. poly-A tail. What is intron? (Page 354) A. Removal of introns. What is the specific inhibitor of RNAP? (Page 352) A. It is also called pribnow box. The specific signals are recognised by a termination protein. How termination of transcription is effected? (Page 353) A. adding poly A tail at 3' end and methylation. This is effected by an interrupted invert repeat in DNA. What are the non-coding sequences? (Page 354) A. Leader sequence. Part of mRNA that is removed is called intron. addition of a cap at 5' end. It is a signal for initiation of transcription in prokaryotes. the Rho factor. Q. Q. . What is TATA Box? (Page 352) A. Q. It is about 10 bp upstream of starting of mRNA synthesis. Q. Godberg-Hogness Box.Molecular Biology-III 221 Q. What is the direction of transcription?(Page 352) A. What is the corresponding signal in mammals? (Page 352) A.
Rifampicin. Spliceosomes. What is the mechanism of action of Rifampicin? (Page 354) A. What is a spliceosome? (Page 354) A. Q. Q. Give the names of inhibitors of RNA synthesis. What are ribozymes? (Page 354) A. thus blocking transcription. What is the cause for systemic lupus erythematosis? (Page 354) A. Q. Q. (Page 354) A. They are used as anticancer drugs. RNAse-P (which generates the ends of tRNAs) and peptidyl transferase (present in ribosomes) are examples of ribozymes. a fatal autoimmune disease. Q. Actinomycin D and mitomycin intercalate with DNA strands. mitomycin and amanitin. This is taking place inside the nucleus. Enzymes made up of RNA are called ribozymes. It binds to beta subunit of RNA polymerase. Small nuclear ribonucleoprotein particles (SnRNPs) associated with hnRNA at the exonintron junction form spliceosomes. Q. and inactivates it. Rifampicin is widely used in the treatment of tuberculosis and leprosy. . actinomycin. (Page 354) A. What is the mechanism of action of mitomycin? (Page 354) A. Give some examples of ribozymes. Production of auto antibodies against small nuclear ribonucleoprotein particles cause systemic lupus erythematosis (SLE).222 Viva—based on Textbook of Biochemistry Q.
The human immunodeficiency virus (HIV) causing AIDS is a retrovirus. During transcription. (Page 355) A. It has clover shape appearance. genetic information is transferred from RNA to DNA.Molecular Biology-III 223 Q. (Page 355) Q. DNA is synthesised in which direction? (Page 356) A. Q. It inactivates RNA polymerase II. DNA polymerase or reverse transcriptase will make a new DNA strand based on the RNA template. What is the mechanism of action of amanitin? (Page 354) A. Amino acid binding is at 3' end. (Page 356) . RNA is the genetic material (not DNA). Thus. amino acid sequence is specified by what? A. The codons present in messenger RNA. From 5' to 3' direction. From 5' to 3' direction. It contains unusual bases. What is reverse transcriptase? (Page 354) A. During protein synthesis. The opposite part has anticodon arm. In retroviruses. Q. Q. Q. The RNA dependent. Q. What are the structural features of tRNA molecule? (Page 355) A. During replication. Give an example of retrovirus. mRNA is synthesised in which direction? A.
From amino terminal end to carboxy terminal end. Q. What is meant by degeneracy of genetic code? (Page 356) A. Q. protein is synthesised in which direction? A. One amino acid is represented by multiple codons. degenerate. (Page 356) Q. Q. Q. What is the initiating codon for protein synthesis? (Page 357) A. Anticodons pair with codons that differ at the third base. but unambiguous and universal. Where is protein biosynthesis taking place? (Page 358) A. . The codons are non-overlapping. Marker of start signal for translation in bacterial mRNA. Q. Triplet codons are consecutive three bases pairs in mRNA. What is Shine-Dalgarno sequence? (Page 357) A. AUG. What is meant by the term wobbling?(Page 357) A.224 Viva—based on Textbook of Biochemistry Q. Q. What are the salient features of genetic code? (Page 356) A. How many high energy bonds are required for the synthesis of one peptide bond? (Page 359) A. or in cytoplasm. Ribosomal assembly either attached to endoplasmic reticulum. During translation. Four high energy bonds.
(Page 360) Q. Give examples of diseases caused by protein targetting defects. What is the function of signal peptide? (Page 360) A. Gamma carboxylation of prothrombin. Give examples for post-translational modifications. (Page 361) A. adrenoleukodystrophy and primary hyperoxaluria. (Page 361) A. A. (Page 361) . Ehlers-Danlos syndrome. (Page 360) Q.Molecular Biology-III 225 Q. Give examples of inhibitors of translation in eukaryotic cells? A. What is the location of signal peptide? (Page 360) A. and so directs the new protein into the endoplasmic reticulum. and glycosylation of proteins. Q. Lathyrism. Q. diphtheria toxin. and ricin. Puromycin. hydroxylation of proline in collagen. These are in the carboxy terminal end of proteins. What is the location of the address for destination of proteins? A. Q. Q. methylation of histones. cycloheximide. Causes anchorage of ribosome to endoplasmic reticulum. Zellweger syndrome. and scurvy. Such proteins are destined for secretion. Give examples of diseases produced by defect in post-translational modifications. In the amino terminal region of the nascent protein.
Inhibition of translocation in prokaryotes. . Q. Give an example of irreversible inhibitor of protein synthesis in bacteria. (Page 361) Q.226 Viva—based on Textbook of Biochemistry Q. Streptomycin is an example. chloramphenicol. These antibiotics are bacteriostatic. What is the mechanism of action of tetracycline? (Page 361) A. Tetracyclins. A. Inhibition of peptidyl transferase in bacteria. Misreading of codes and inhibition of initiation complex formation in bacteria. What is the mechanism of action of streptomycin? (Page 361) A. Q. These antibiotics are bactericidal. Due to mutation in mitochondrial DNA. Give examples of reversible inhibitors of protein synthesis in bacteria. Q. Inhibition of tRNA binding to ribosome in bacteria. Leber’s hereditary optic neuropathy is due to what? (Page 362) A. What is the mechanism of action of erythromycin? (Page 361) A. Q. Q. (Page 361) A. What is the mechanism of action of chloramphenicol? (Page 361) A. erythromycin and clindamycin are examples.
glucose-6-phsophate dehydrogenase deficiency. Here. Q. and duchenne type muscular dystrophy. . the normal codon GAG is changed to GUG (transversion). HbS or sickle-cell hemoglobin is produced by a mutation of the beta chain in which the 6th position is changed to valine. What type of mutation is it? (Page 366) A.Molecular Biology-V Molecular Biology-IV 227 Molecular Biology-IV: Molecular Genetics and Control of Gene Expression Q. Give an example. Q. Give examples of X-chromosome linked transmission. What is a mutation? (Page 366) A. Q. (Page 364) A. (Page 366) A. instead of the normal glutamate. An alteration in the genetic material results in a mutation. Hemophilia.
(Page 368) Q. and methyl cholanthrene. What is a prion? (Page 372) A. (Page 366) A. Give examples of enzyme induction. Give names of some important antiviral drugs. X-rays. Q. gamma rays. In which phase of the cell cycle. It is an oncosuppressor gene product. How mutagenecity of a compound is tested? (Page 367) A. “Prions” is the acronym for “proteinaceous infective particles”. Give an example for an unacceptable mutation. What is the p53? (Page 368) A. S phase. A. Zidovudine. (Page 367) A. Q. Beta galactosidase by lactose. Q. Q. By Ame’s test. DNA synthesis is maximum? A. tryptophan pyrrolase by glucocorticoid and ALA synthase by barbiturates. (Page 371) A. Acyclovir. Haemoglobin M. Give an example of repression. (Page 370) A. Acridine orange. .228 Viva—based on Textbook of Biochemistry Q. Q. Q. Ribavirin. ALA synthase by heme. (Page 370) Q. Give examples for mutagens.
What are the uses of recombinant DNA technology? (Page 374) A. especially human proteins. (Page 375) . Restriction endonuclease. Risk of contamination is eliminated. Restriction endonucleases are referred to as “molecular scissors”. They are useful in recombinant DNA technology. Quantitative preparation of bio-molecules. These enzymes recognise specific sequence with palindrome arrangement in the double stranded DNA. and DNA ligase. Q. when preparing such biomolecules. and then cleave at those sites. plasmid vector. What are restriction endonucleases? (Page 374) A. What are required for preparing a recombinant DNA molecule? A.Molecular Biology-V 229 Molecular Biology-V: Recombinant DNA Technology and Gene Therapy Q. It is used in gene therapy. Specific probes for diagnosis of diseases can be prepared. Q.
cut pieces are electrophoresed in agarose gel. (Page 379) A. Duchenne muscular dystrophy. when single-stranded DNA will be adsorbed in the nitrocellulose membrane. In this technique. What is Northern blotting? (Page 379) A. The radio active probe is placed over the membrane.230 Viva—based on Textbook of Biochemistry Q. What is Western blotting? (Page 379) A. Q. prenatal diagnosis. then blotted over to a nitrocellulose membrane. Give some examples of genetic diseases that could be identified by Southern blotting. Q. to demonstrate virus integration. The proteins are isolated from the tissue and electrophoresis is done. fragmented by restriction endonucleases. What is the use of Southern blotting?(Page 378) A. How are DNA fragments separated? (Page 378) A. DNA is isolated. Sickle cell anemia. The Northern blot is used to demonstrate specific RNA. To identify abnormal genes. it is probed with radioactive antibody and auto-radiographed. Agarose gel electrophoresis. What is Southern blotting? (Page 378) A. Q. . Huntington’s chorea. Q. Q. The membrane is then thoroughly washed and autoradiographed. The separated proteins are then transferred on to a nitrocellulose membrane. After fixation. proteins (not nucleic acids) are identified.
What are the applications of cloning of animals? (Page 379) A. It has medico-legal application. Animals with genetically desirable traits could be bred more efficiently. e. When a cell from an animal is grown to an exact duplicate of that animal. Give some diseases in which gene therapy is used successfully? A.Molecular Biology-V 231 Q.g. Q. When a gene of higher organism is introduced into a bacterial DNA. it is called “cloning of the gene” or “molecular cloning”. What is the application of DNA fingerprinting? (Page 381) A. What are the vectors used for gene therapy? (Page 381) A. Severe combined immuno deficiency. cystic fibrosis. Cows or goats may be genetically engineered to produce milk containing any human protein. Q. adenovirus. Q. Locating mutations in DNA. What is meant by the term cloning? (Page 379) A. RFLP (restriction fragment length polymorphism) is used for what? A. Retrovirus. it is known as “cloning of an animal” or “somatic cloning”. familial hypercholesterolemia. (Page 381) Q. duchenne muscular dystrophy. Q. The term cloning has two broad meanings. and plasmid liposome complex. cows yielding more milk.(Page 382) . and hemophilia.
A recombinant DNA segment. What is transgenesis? (Page 383) A. Only very minute quantity of sample is required. But in reverse PCR. DNA is detected. especially prenatal diagnosis. Taq polymerase. (Page 384) Q. Diagnosis of bacterial and viral diseases. medicolegal cases. containing the desired gene from another species. is introduced into the fertilized ova. Polymerase chain reaction. that means. Q. it is derived from a living organism. What is the use of PCR? (Page 384) A. that DNA could be from a living or non-living organism. Which enzyme is required for PCR (polymerase chain reaction)? A. Q. It is a form of germ cell gene therapy. mRNA is detected. In ordinary PCR.232 Viva—based on Textbook of Biochemistry Q. . What is the technique used for gene amplification? (Page 384) A. The embryos are allowed to develop in the uterus of another animal. Q. This allows cDNA synthesis from mRNA followed by PCR amplification. What is reverse PCR? (Page 384) A. diagnosis of genetic disorders.
To rule out the false positive test. (Page 388) . What is the full form of AIDS? (Page 387) A. is then retested with Western blot analysis. Q. What is the causative organism of AIDS? (Page 387) A. Human immunodeficiency virus. the ELISA positive blood. What are the usual laboratory findings in the diagnosis of AIDS? A. Q. In the window period viral capsid antigen (p24) can be detected Q. The antibodies against gp120 are detected by the ELISA test. Acquired immuno deficiency syndrome. How can you detect window period of the disease? (Page 387) A.Clinical Biochemistry-III Biochemistry of AIDS 233 233 Biochemistry of AIDS Q.
234 Viva—based on Textbook of Biochemistry Q. HIV belongs to which group of virus?(Page 388) A. while a count more than 1 lakh per ml means very bad prognosis. . By RTPCR (reverse transcriptase polymerase chain reaction. Where is CD4 molecules present? (Page 388) A. Q. Reverse Transcriptase (RT) inhibitors and protease inhibitors. How RT inhibitors are classified? (Page 390) A. the number of HIV particles in blood can be estimated.mm. What are the major groups of anti-HIV drugs available? (Page 390) A. How the virus gets entry into the tissue cells? (Page 388) A. Q. What other special tests could be done? (Page 388) A. Q. Q. The CD4 molecules are present on the surface of T-helper cells. nucleoside analogues. Q. The gp 120 of the virus envelope will specifically bind with CD4 molecules on the surface of target cells. Q. CD4 acts as a receptor for the virus. It is a retrovirus. It is an RNA virus. non-nucleoside analogues and nucleotide analogues. a value of less than 5000 copies per ml of blood has good prognosis. It contains the enzyme reverse transcriptase. T-helper cell count is below 300/ cu. What is the characteristic of retrovirus? (Page 388) A.
X-ray. Genes capable of causing cancer. Oncogenes are specific sequences in DNA which when expressed may produce cancer. (Page 393) A. What are Oncogenes? (Page 394) A. hepatitis B virus(HBV). (Page 393) Q. Vitamin E. Vitamin C. Oncogenes present in normal cells are also called as proto-oncogenes. A. and human papilloma virus. Q. Name some oncogenic viruses. (Page 393) A. Q. What are proto-oncogenes? (Page 394) A. Epstein Barr virus (EBV). benzopyrenes. . Q. gamma-ray and UV-ray. Q. and curcumin.Clinical Biochemistry-III Biochemistry of Cancer 235 235 Biochemistry of Cancer Q. Name some physical carcinogens. Methyl cholanthrene. aflatoxins. Name some anti-mutagens and anti-carcinogens. Name some chemical carcinogens. (Page 391) A. Vitamin A.
and regan iso-enzyme of alkaline phosphatase. Alpha feto protein. (Page 399) Q. . Q. What is the clinical application of tumour markers? (Page 398) A. Viral infection. produced by the deletion of an oncosuppressor gene? A. They are useful for the following purposes. (Page 399) A. beta chain of human chorionic gonadotropin. Retinoblastoma. (2) To detect the recurrence of the tumour Q. Q. Name some important tumour markers. Colorectal and gastrointestinal cancers. which could be detected in blood and therefore indicate the presence of the tumour in the body. mutation in proto-oncogene. neuron specific enolase. and chromosome translocation. carcino embryonic antigen. Name a cancer. Alpha feto protein (AFP) level in serum is increased in which condition? A. promoter insertion. Carcino embryonic antigen level is increased in which type of cancers? (Page 399) A. Hepatoma. What are tumour markers? (Page 398) A. Proto-Oncogenes may be activated by what mechanisms? (Page 395) A.236 Viva—based on Textbook of Biochemistry Q. prostate specific antigen. Q. They are factors released from the tumour cells. (Page 396) Q. (1) For follow up of cancer and to monitor the effectiveness of the therapy.
. Q. Q.Clinical Biochemistry-III Biochemistry of Cancer 237 237 Q. What is the mechanism of action of mitomycin? (Page 400) A. It is a folic acid antagonist. Q. What is the mechanism of action of adriamycin? (Page 400) A. so they are used as anti-cancer drug. Intercalation with DNA strands. they interfere with assembly of cytoskeleton and inhibits stathmokinesis (spindle movement). It is a tumour marker for choriocarcinoma. Q. It inhibits topo-isomerase. What is the significance of beta chain of human chorionic gonadotropin? (Page 399) A. What is vincristine and vinblastine? (Page 400) A. What is the mechanism of action of Methotrexate? (Page 400) A. They are alkaloids from vinca rosea.
Gamma radiation.238 Viva—based on Textbook of Biochemistry Applications of Radio-isotopes in Medicine Q. Isotopes of a given element will have different atomic weights. Q. Q. Q. What is the isotope used for DNA studies? A. What is an Isotope? A. Q. To treat polycythemia vera. Iodine-125 emits mainly emits which type of radiation? A. but will have same atomic number. Alpha radiation. P-32 is used clinically for what purpose? A. . P-32. Radiation hazard is mainly due to which type of radiation? A.
Q. 131-Iodine labelled hippuran. 137-Cs (caesium) with a half-life of 30 years.Applications of Radio-isotopes in Medicine Clinical Biochemistry-III 239 239 Q. such as carcinoma cervix or body of uterus. Intracavity application of radiation. Q. Q. Lymphomas. What is the use of radio active radium in medicine? A. Q. What are the important toxic effects of radiation? A. Hodgkin’s disease and neuroblastoma are highly radiosensitive. . and radiation dermatitis. Which radio-active compound is used to measure glomerular filtration rate (GFR)? A. What is the common source of radiation in teletherapy? A. 125-Iodine. Leukopenia. the radio-active isotope used is: A. thrombocytopenia. Q. What are radiosensitive tumours? A. For RIA (radio immuno assay).
. protein is to be diluted and carbohydrate is to be added. The lactose synthase has two subunits. This will make it comparable to human milk. What is the major difference between human and cow’s milk? A. How lactose synthesis is regulated? (Page 407) A. How lactose is synthesised? (Page 407) A. Thus.240 Viva—based on Textbook of Biochemistry Body Fluids Q. This synthesis of lactose in mammary gland is catalysed by lactose synthase. a catalytic subunit which is a galactosyl transferase and a modifier subunit that is alpha lactalbumin. UDP glucose is epimerased to UDP galactose. Human milk has higher carbohydrate content than cow’s milk while protein content is less. (Page 407) Q. The level of the modifier subunit is under the control of prolactin. Q. to one cup of cow’s milk. Q. How is to humanize cow’s milk? (Page 407) A. add half a cup of water and two teaspoons of sugar. Then the galactose unit is transferred from UDPgalactose to glucose. To humanise cow’s milk.
(Page 407) Q. The fatty acids are mainly saturated. Q. but 50% of them are medium chain fatty acids (Lauric and Myristic acids). . Q. Q. What type of protein is casein? A. the casein is precipitated (iso-electric precipitation). What are the proteins present in whey? (Page 407) A. If milk is acidified and pH lowered to 4. Eighty percent protein of cow’s milk is casein.Body Fluid Clinical Biochemistry-III 241 241 Q. Q. Lactalbumin. They are easily digested. What is the advantage of medium chain fatty acids? (Page 407) A. How the phosphate group is attached to protein? (Page 407) A. Q. lactoglobulin and lysozyme. The phosphate groups are added to the hydroxyl groups of serine or threonine residues. The supernatant is called whey. absorbed and metabolized. What is the major protein in cow’s milk? (Page 407) A. What is whey? (Page 407) A.7. Milk contains which type of fatty acids? (Page 407) A. It is a phospho-protein.
Adenyl cyclase will produce cyclic AMP. and binding of hormone causes activation of G protein. How adenyl cyclase is destroyed? A. (Page 411) . Q. Q. How is G protein activated? (Page 411) A. and thereby G protein is activated. Binding of hormone on receptor causes attachment of GTP to G protein.242 Viva—based on Textbook of Biochemistry Hormones-I: Mechanism of Action of Hormones Q. How the G proteins work? (Page 410) A. Q. What is the function of adenyl cyclase? (Page 411) A. The receptors are in membrane. What is the function of activated G protein? (Page 411) A. Q. Activated G protein activates adenyl cyclase. What are G proteins? (Page 410) A. By phospho diesterase. Q. They are involved in signal transduction.
How cyclic AMP further works? (Page 411) A. ANF (atrial natriuretic factor). What is the function of protein kinase? (Page 411) A. . Q. Q. Q. estrogens. Q. and calcium. androgens. ADH. FSH. Name some second messengers. Name some hormones that bind to intracellular receptors. Cyclic AMP activates protein kinase. 1.2-diacyl glycerol. and thyroxin. mineralocorticoids. (Page 410) A. inositol triphosphate. progesterone. (Page 413) A. (Page 410) A. Name some hormones which act through cyclic GMP as the second messenger. Cyclic AMP. It phosphorylates enzymes or target proteins. Name some hormones which act through cyclic AMP as the second messenger.Hormones-I Clinical Biochemistry-III 243 243 Q. Glucagon. TSH. LH. Q. ACTH. Glucocorticoids. so that they are activated. (Page 412) A.
Q. and beta chains are specific.244 Viva—based on Textbook of Biochemistry Hormones-II: Pituitary Hormones Q. and PIF (prolactin inhibitor factor). Q. CRF (corticotropin releasing factor). FSH. These neurohormones are antidiuretic hormone (ADH) and oxytocin. TSH. TRH (thyrotropin releasing hormone). GnRH (gonadotropin releasing hormone). GHRH (growth hormone releasing hormone). LH and HCG have the common alpha chain. Name the important hypothalamic releasing factors. somatostatin (growth hormone inhibitory factor). . (Page 415) A. What are hypothalamic neuropeptides? (Page 414) A. Alpha chain of human chorionic gonadotropin (HCG) is shared with what else? (Page 415) A.
(Page 415) Q. GH (Growth hormone). Deficiency of GH secretion in early childhood results in pituitary dwarfism. and PRL (Prolactin). and produces positive nitrogen balance. What is the function of LH? (Page 416) A. ACTH (Adrenocorticotropic hormone). LH (Luteinising hormone). Testosterone in males (secreted by Leydig interstitial cells) and progesterone in females (secreted by corpus luteum). What are the hormones produced by anterior pituitary? (Page 415) A. Q. Increased secretion of growth hormone will lead to what condition? A. The overall effect of GH is to stimulate growth of soft tissues. Q. cartilage and bone. What is the major effect of growth hormone? (Page 415) A.Hormones-II Clinical Biochemistry-III 245 245 Q. . Q. TSH (Thyroid stimulating hormone). enhances protein synthesis. The anti-insulin effect of GH causes lipolysis and hyperglycemia. Q. MSH (Melanocyte stimulating hormone). are increased under the influence of LH. What is the function of FSH? (Page 416) A. FSH (Follicle stimulating hormone). FSH stimulates growth of ovarian follicles in females and spermatogenesis (Sertoli cells) in males. GH increases the uptake of amino acids by cells. It is anabolic. Excess secretion of GH secretion leads to gigantism in children and acromegaly in adults. What is the result of decreased growth hormone secretion? (Page 415) A.
Cortisol has how many carbon atoms?(Page 417) A. Q. Which is the precursor of steroid hormones? A. The 11-hydroxylase is required for the synthesis of which hormone? A. The 17-hydroxylase is required for the synthesis of which hormones? A. 21. and estrogens. Aldosterone has how many carbon atoms? (Page 418) A. (Page 417) Q. What are the hormones produced from progesterone? (Page 417) A. (Page 417) Q. testosterone. Corticosterone. and estradiol.246 Viva—based on Textbook of Biochemistry Hormones-III: Steroid Hormones Q. Q. 21. (Page 417 and 418) Q. . Cortisol. testosterone. Cholesterol. aldosterone. Cortisol.
and depressed immune function . and hydroxyl groups on 3rd and 17 carbon atoms. Q. 19. Q. Q. total 18 carbon atoms. Cyclopentanophenanthrene ring. (Page 418) Q. Increased gluconeogenesis. 18.Clinical Biochemistry-III Hormones-III 247 246 Q. Testerone has how many carbon atoms? (Page 418) A. aromatic character of A ring. What are the effects of glucocorticoids? (Page 419) A. Estrogen has how many carbon atoms? (Page 418) A. Testosterone. elevated protein breakdown. What are the structural features of estradiol? (Page 418) A. What is the immediate precursor of estrogens? (Page 418) A. augmented lipolysis. 21-hydroxylase is required for the synthesis of which hormone? A. Q. Aldosterone.
and methimazole. Q. Tyrosine residues of thyroglobulin are iodinated. Blood concentration of T4 is 70 times more than of T3. What is the ratio of T4 and T3 in blood? (Page 424) A. How thyroid hormones are produced?(Page 423) A. Q.248 Viva—based on Textbook of Biochemistry Hormones-IV: Thyroid Hormones Q. What is the precursor of thyroxin? A. Tyrosine. enhances the oxidation of iodine to iodide. It increases the uptake of iodine by thyroid gland. Q. (Page 423) Q. (Page 423) A. perchlorate. and favours the hydrolysis of thyroglobulin to produce T4. What is the function of thyroid stimulating hormone? (Page 423) A. . Name some antithyroid agents. Thiocyanate.
Gluconeogenesis and carbohydrate oxidation are increased. fine tremors. What are the salient features of hypothyroidism? (Page 426) A. Glucose tolerance test shows rapid absorption. Q. anxiety and sensitivity to heat. Thyroxine in large quantities can swell the mitochondria. What are the biochemical features of thyroid hormones? (Page 424) A. Q. diarrhea. increased TSH level. emotional disturbances. tachycardia. Myxedema. Decreased T3 level. sweating. Q. High TSH and T4 levels.Clinical Biochemistry-III Hormones-IV 249 249 Q. Fatty acid metabolism is increased. How this is produced? (Page 424) A. Q. What are the functions of thyroid hormones? (Page 424) A. increased rate of metabolism. Deficiency of thyroxine results in which condition? (Page 426) A. What are the characteristic features of primary hyperthyroidism? A. lethargy. hypercholesterolemia. Q. Thyroxine increases cellular metabolism. The thermogenic effect is mediated by uncoupling of oxidative phosphorylation. Calorigenic effect or thermogenesis and BMR is increased. weight gain. (Page 426) . Basal metabolic rate (BMR) is increased. weight loss. and decreased basal metabolic rate.
thymol. Why sodium fluoride is used as a preservative of blood for glucose estimation? (Page 427) A. toluene. What is optical density? A. What are the preservatives used in urine sample? (Page 427) A. Optical density = minus logT. Q.250 Viva—based on Textbook of Biochemistry Clinical Biochemistry-I Q. chloroform. concentrated HCl and glacial acetic acid are the commonly used urine preservatives. Q. What is Beer-Lambert’s law? (Page 428) A. Formalin. . the intensity of the colour is directly proportional to the concentration of the coloured particles in the solution. (Page 428) Q. The Lambert’s law states that the amount of light absorbed by a coloured solution depends on the length of the column or the depth of the liquid through which light passes. As per Beer’s law. To prevent glycolysis and to prevent loss of sugar.
Q. . Accuracy is the closeness of a result to the true value. What is meant by the term precision? (Page 430) A. Precision depends on the technique. as well as on the technician. Precision refers to the reproducibility of the result. Serum sample and reagents are mixed and incubated for a fixed time. Q. Specificity of a reaction denotes that only one substance will answer that particular test. Then. What is meant by specificity? (Page 430) A.Clinical Biochemistry-III Clinical Biochemistry-I 251 Q. This is called end point analysis. Serum and reagents are incubated. What is kinetic method? (Page 429) A. What is accuracy? (Page 430) A. and from the difference in OD between the two values. the OD is ascertained and the concentration of the substances is calculated. Q. but is quicker and hence is often used in autoanalysers. Q. to develop the colour optimally. What is end point analysis? (Page 428) A. the reagents. Here the optimum colour is not developed. and readings are taken at 2 and 3 minutes exactly. the concentration is calculated. Specificity is determined by the method of the analysis.
. Q. Q. Serum bilirubin between 1 mg/dl and 2 mg/dl. What is the normal serum bilirubin level? (Page 431) A. 0. What is the normal serum level of conjugated bilirubin? (Page 431) A.6 mg/dl.2 mg/dl. Q. Less than 0. What is the normal blood level of unconjugated bilirubin? (Page 431) A.252 Viva—based on Textbook of Biochemistry Clinical Biochemistry-II: Liver and Gastric Function Tests Q. 0. Jaundice appears if the serum bilirubin goes above 2 mg/dl. What is latent jaundice? (Page 431) A.8 mg/dl.2 to 0. Q. Jaundice appears at what level of bilirubin? (Page 431) A.2-0.
When bilirubin is conjugated. urine bile salts. When the bilirubin is unconjugated. Serum bilirubin. and this response is known as indirect positive. What is meant by van den Bergh’s direct positive test? (Page 431) A. a biphasic reaction is observed. Q. conjugated bilirubin in serum is elevated. the purple colour is produced immediately on mixing with the reagent. Q. . unconjugated bilirubin is increased in serum. the colour is obtained only when alcohol is added. Q. What about hepatocellular jaundice? (Page 431) A. albumin. bile pigments and urobilinogen. Q. In hepatocellular jaundice. Hence van den Bergh’s test is indirect positive. In obstructive jaundice. the response is said to be van den Bergh’s direct positive. alkaline phosphatase. and van den Bergh’s test is direct positive. What happens in obstructive jaundice? (Page 431) A.Clinical Biochemistry-III Clinical Biochemistry-II 253 Q. What type of bilirubin is present in hemolytic jaundice? (Page 431) A. In hemolytic jaundice. What are important liver function tests? (Page 432) A. because both conjugated and unconjugated bilirubins are increased in serum. What is indirect positive van den Bergh’s test? (Page 431) A. Q.
Serum albumin is lowered. (Page 433) Q. (Page 434) . Increase in serum unconjugated bilirubin occurs in which condition? A. What are the important stimulants for gastric acid secretion? A. Q. What are the enzymes useful in diagnosis of liver diseases? (Page 433) A. and prothrombin time is prolonged. Q. alkaline phosphatase. Which tests will be positive in a urine of a patient with obstructive jaundice? (Page 433) A. Gastrin. presence of bile salts and bile pigments in urine. What are the features of obstructive jaundice? (Page 433) A. and histamine. What is the characteristic laboratory findings in alcoholic cirrhosis? A. and Fouchet’s test. Q. Gmelin’s test. and gamma glutamyl transferase. albumin globulin ratio is reversed. increased alkaline phosphatase level in blood. (Page 433) Q. Hay’s test. Hemolytic jaundice. vagus stimulation. What are the salient laboratory findings in a patient with chronic liver disease? (Page 433) A. Elevation of gamma glutamyl transferase level in serum. Alanine amino transferase. and increased cholesterol in blood.254 Viva—based on Textbook of Biochemistry Q. Q. Elevated conjugated bilirubin in plasma.
bicarbonate level within the cell increases (formed from H2CO3). carcinoma of stomach. What is basal acid output? (Page 435) A. Q.Clinical Biochemistry-II Clinical Biochemistry-III 255 Q. Pernicious anemia. Q. Q. It is the acid output in millimol per hour. When HCl is produced in stomach. 30 mmol/ hour in females and 45 mmol/hour in males. What is the upper limit of basic acid output? (Page 435) A. after the stimulation. 5 millimol/hour in females and 10 millimol in males. it is reabsorbed into blood stream. What is the upper limit of maximal gastric acid output? (Page 435) A. What is the maximal gastric acid output? (Page 435) A. immediately after meals. Q. in the absence of all intentional stimulation. Hypo-acidity is found in which conditions? (Page 435) A. What is alkaline tide? (Page 434) A. and atrophic gastritis. This would account for the alkaline tide of plasma and urine. It is the acid output in millimol per hour. Q. .
(Page 438) .015 to 1. What is the minimum and maximum specific gravity of urine? A.032. Q. Q. What is the normal specific gravity of urine? (Page 438) A. while the cells and proteins are retained in the blood.003 to 1. Q. An ultrafiltrate of the blood is produced in glomerulus. Blood level of 180 mg/ dl. 1. What is the normal renal threshold value for glucose? (Page 437) A. 1.025. How much is glomerular filtration rate? (Page 436) A. What is the function of glomerulus? (Page 436) A. Q. 120-125 ml per minute.256 Viva—based on Textbook of Biochemistry Clinical Biochemistry-III: Kidney Function Tests Q.
ketone bodies. polyuria. Diabetes mellitus.010. What is micro-albuminuria? (Page 439) A.Clinical Biochemistry-III 257 Q.010. Acute glomerulonephritis. and chronic renal failure. (Page 439) Q. blood. What are the features of chronic renal failure? (Page 439) A. Q. Q. nephrotic syndrome. Specific gravity of urine increased in which condition? (Page 439) A. What is the specific gravity of urine in chronic renal failure? A. Which test is commonly employed to detect urinary protein? A. Protein. pyelonephritis. bile pigments. Heat and acetic acid test. . sugar. Urine with fixed specific gravity of 1. Q. (Page 439) A. bile salts. Proteinuria is seen in which conditions? (Page 439) A. and urobilinogen. Polyuria is seen in which conditions?(Page 439) A. increased blood urea and creatinine. and multiple myeloma Q. Acute glomerulo nephritis. diabetes insipidus. Fixed to 1. Q. When small quantities of albumin (50-300 mg/ day) is seen in urine. Name abnormal substances seen in urine. (Page 439) Q.
Inulin clearance. Para amino hippurate (Diodrast) clearance. What is the best method for assessing glomerular filtration rate? A. Clearance is defined as the quantity of blood or plasma completely cleared of a substance per unit time and is expressed as milliliter per minute. nephron loss proteinuria.258 Viva—based on Textbook of Biochemistry Q. Glomerular proteinuria. About 700 ml/min. (Page 441) Q. Creatinine is formed spontaneously (nonenzymatic). Q. Creatinine clearance test. Inulin has to be infused intravenously throughout the test period. How proteinurias are classified? (Page 439) A. Q. (Page 442) Q. What is its disadvantage? (Page 441) A. What is the advantage of creatinine test? (Page 442) A. overflow proteinuria. How renal plasma flow is measured? (Page 441) A. and urogenic proteinuria. What is meant by renal clearance? (Page 441) A. What is the normal value for PAH clearance ? (Page 442) A. Q. Q. so the blood level and excretion rate of creatinine is a constant from day to day. . Q. What is the correct method for assessing glomerular filtration rate? A. It is the ml of plasma which contains the amount of that substance excreted by the kidney within a minute. tubular proteinuria.
. What is the significance of creatinine coefficient? (Page 442) A. 75 ml/minute. 0. A decreased creatinine clearance is a very sensitive indicator of a reduced glomerular filtration rate. Q. Q.7-1. Normal range is 20-28 mg/kg for males and 1521 mg/kg for females. What is the normal creatinine level in blood? (Page 442) A. Urea clearance is lowered in which condition? (Page 443) A. What is the normal value of creatinine coefficient? (Page 442) A. for adult females. Q. Q.Clinical Biochemistry-III 259 Q.3 mg/dl.4 mg/dl. What is the maximum urea clearance value? (Page 443) A.6-1. Q. Q. What is the normal value of creatinine clearance? (Page 442) A. It is the urinary creatinine expressed in mg/kg body weight. Chronic liver failure. The value is elevated in muscular dystrophy. Q. 0. In males 85-125 ml/min and in females 80-115 ml/ min. What is the significance of creatinine clearance? (Page 442) A. What is creatinine coefficient? (Page 442) A. For adult males.
How failure of concentrating capacity of urine is measured ? A. 54 ml/minute. Measurement of specific gravity. acidification test. Q. concentration test. When the volume of urine formed is less than 2 ml per minute. Urine specific gravity. Concentration test (Water deprivation test). Q. 20-40 mg /dl. What are the usual tests to assess tubular function? (Page 444) A. Urea level is increased in renal failure. Q.(Page 443) Q. What is the normal blood urea level? (Page 443) A. What is the clinical significance of increased urea level in blood ? A. What is the standard urea clearance value? (Page 443) A. (Page 444) Q. dilution test. . Q.260 Viva—based on Textbook of Biochemistry Q. How is tubular concentrating capacity measured? (Page 444) A. When do you call it standard urea clearance? (Page 443) A.
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