Biochemistry Q P 2011 - 2023

1079_2011_1_S263
Rajiv Gandhi University of Health Sciences

M.B.B.S. PHASE - I Degree Examination - June / July 2011
Time: 3 Hours [Max. Marks: 100]
BIOCHEMISTRY (RS 2 & RS 3)
QP Code: 1079 – PAPER I (Max. Marks: 50)
Your answer shall be specific to question asked. Draw neat and labelled diagrams wherever
necessary. Use separate answer books for section A and section B.
LONG ESSAY 1 X 10 = 10 Marks

1. Discuss the formation and fate of ketone bodies
SHORT ESSAY 5 X 5 = 25 Marks

2. Glycogenolysis
3. Decarboxylation of amino acids
4. Diagnostic uses of enzymes
5. Fatty acid synthase complex
6. Detoxification by oxidation
SHORT ANSWERS 5 X 3 = 15 Marks

7. Free radicals and disease
8. Active transport
9. Essential amino acids
10. Any three enzymes unique to gluconeogenesis
11. Uncouplers of oxidative phosphorylation
QP Code: 1080 – PAPER II (Max. Marks: 50)

Use separate answer book

1. What is genetic code. Describe the process of eukaryotic translation

2. Nitrogen balance
3. Functions of albumin
4. Biochemical functions and deficiency manifestations of vitamin D
5. Functions of iodine
6. Structure of mRNA

7. Types and causes of beri – beri
8. Causes of sickle cell anemia
9. Immunoglobulin A (IgA) and immunoglobulin M (IgM)
10. Describe any three renal function tests
11. What is orotic aciduria? Explain the biochemical basis of manifestation
*****
~-
~~'~
, 1079 20 I I 2 S265.doc
Rajiv Gandhi University of Health Sciences

M.B.B.S. PHASE - I Degree Examination - Dee 2011 / Jan 2012
Time: 3 Hours [Max. Marks: 100]
BIOCHEMISTRY (RS 2 & RS 3)

QP Code: 1079 - PAPER I (Max. Marks: 50)
Your answer shall be specific to question asked. Draw neat and labelled diagrams wherever necessary.
Use separate answer books for section A and section B.

1. Describe the reactions of Urea cycle. Discuss the interrelation of urea cycle and citric acid cycle.
What is the reference range for serum urea?

2. Classify transport mechanisms across cell membranes. Define uniport, symport and antiport. Give
an example of each
3. Define primary, secondary, Tertiary and Quarternary structure of protein. What are the noncovalent
forces which preserve the secondary structure
4. Explain the mechanism of action of Allosteric Enzymes? Name the Allosteric Inhibitor and Allosteric
Activator for Phosphofructokinase and Acetyl CoA - Carboxylase
5. Outline the steps for synthesis of cholesterol. Discuss the rate limiting step and regulation of
synthesis of cholesterol
6. Describe the reactions of Citric Acid cycle
SHORT ANSWERS 5 X 3 = 15 r-.1arks
7. Oncogenes
8. Thyroid function tests - Routine and anti - TPO
9. Cytochromes
10. GTT Graph for Renal Glycosuria
11. Anti - oxidants
QP Code: 1080 - PAPER II (Max. Marks: 50)

Use separate answer book
What is qluconeoqc.x-crs? Describe the pathway in detail and add a note on its significance

2. Briefly outline the steps of Denovo synthesis of purine
3. Hormonal regulation of Fluid and Electrolyte
4. Briefly explain the renal mechanisms involved in maintenance of pH of blood
5. Sources, biochemical role and dietary requirement of vitamin A
6. Protein Calorie malnutrition

7. Operon concept
8. Bence jones proteins
9. What is porphyria? Mention the defect and signs and symptoms of acute intermittent porphyria
10. Enumerate three functions of the liver and three tests with reference ranges to assess them
11. What is a Chimeric DNA molecule. Give the applications of recombinant technology
**** *
Rajiv Gandhi University of Health Sciences, Karnataka
First Phase MBBS Degree Examination – June 2013
Time: Three Hours Max. Marks: 100 Marks
BIOCHEMISTRY (RS2 & RS3)
QP Code: 1079 – Paper I (Max.Marks:50)
Your answers should be specific to the questions asked
Draw neat labeled diagrams wherever necessary
Use separate answer books for section A and Section B
LONG ESSAYS 1 x 10 = 10 Marks

1. What are enzymes? Classify enzymes with one example each. Explain any four factors that
affect enzyme activity.
SHORT ESSAYS 5 x 5 = 25 Marks

2. Define gluconeogenesis. How is alanine converted to glucose?
3. What is substrate level phosphorylation? Give two examples with complete reaction.
4. Classify lipoproteins and write the functions of each lipoprotein.
5. What are transamination reactions? Giving two examples discuss the importance of these
reactions.
6. Classify proteins based on their function giving an example for each class.
SHORT ANSWERS 5 x 3 = 15 Marks

7. High energy compounds
8. Glycogen storage disorders.
9. Enzymes of diagnostic importance
10. FIGLU excretion test
11. Mitochondrial shuttle systems.
*****
QP Code: 1080 – Paper II (Max.Marks:50)

1. What are sources of C & N atoms of purine? Describe the biosynthesis of purine and add a note
on its regulation.

2. Name the different types of RNA. Write their salient features. Mention their functions.
3. What are buffers? Discuss any two buffer system of the body.
4. Give the biochemical functions of niacin with examples and manifestation of its deficiency.
5. What is a restriction endonuclease? Explain their role in recombinant DNA technology.

6. Give an account of phosphorus metabolism.

7. Post translational modifications
8. Base pairing rule and Wobble hypothesis.
9. Biochemical defect in Thalassemia.
10. Cause of Scurvy and beri beri.
11. Creatinine clearance test.
*****
Rajiv Gandhi University of Health Sciences, Kamataka
First Phase MBBS Degree Examination - Dee 2013 ~S-
QP Code: 1079 - Paper I (Max.Marks:SO)
LONGESSAYS 1 x 10 = 10 Mark~
1. Describe the citric acid cycle. How is it regulated? Write about its energetic and amphibolic
nature.
SHORTESSAYS 5x 5 = 25 Mark~
2. Describe the fate and functions of methionine.
3. What are the reactions of HMP pathway? What is the significance of this pathway?
4. Clinical importance of enzymes in assessment of cardiac disease & liver function
5. Outline the de novo synthesis of fatty acid. What are the advantages of having a multifunctional
enzyme complex?
6. How is urea synthesized in the body? Give the reactions. What is the significance of urea cycle?
SHORTANSWERS 5x 3 = 15 Mark~
7. Phospholipids.
8. Coenzymes.
9. Secondary structure of proteins.
10. Prostaglandins.
11. Transamination
*****
Rajiv Gandhi University of Health Sciences, Kamataka
First Phase MBBS Degree Examination - Dee 2013 <JJ
QP Code: 1080 - Paper II (Max.Marks:50)
LONGESSAYS 1 x 10 = 10 Marks
1. Describe the synthesis and breakdown of haemoglobin. Write a note on haemoglobinopathies.
SHORTESSAYS 5x 5 = 25 Marks
2. Explain the structure of tRNA with diagram and mention its function.
3. Define BMR. How do you calculate BMR? Discuss four factors that effect BMR.
4. Describe with an example regulation of gene expression.
5. What do you mean by gene therapy? Discuss its application in medicine.

6. Describe the catabolism of purine nucleotide. Add a note on Gout.
SHORTANSWERS 5x 3 = 15 Marks
7. Anticancer agents
8. Plasmids and oncogenes
9. Obstructive jaundice and its diagnosis
10. Abnormal components of urine
11. Radio isotopes.
*****

1. Classify amino acid based on their structure giving examples.

2. What is an allosteric enzyme? Describe with two examples.
3. Discuss the Embden-Mayerhof pathway that occurs in RBC. Add a note on its energetics.
4. What are lipoproteins? Name the lipoproteins and give their functions.
5. What is biotransformation? Discuss the different phases of biotransformation with an example.

6. Describe the biochemical changes that occur during starvation.
Or
Components of electron transport chain

7. Pyruvate dehydrogenase complex
8. GABA, PUFA and SAM and their importance
9. Importance of iodine
10. Figlu
11. Epimerism and Anomerism.
*****

1.
Define translation. Describe the steps of translation. Name four inhibitors and
their action

2. How is bilirubin formed and excreted? Name the abnormalities associated with bilirubin
metabolism.
3. Describe the liver function tests based on synthetic and excretory role
4. Write the Henderson-Hasselbach equation and its significance in bicarbonate buffer system.
5. Discuss the biochemical changes during starvation

6.
What are nucleotides? What are the sources of C and N atoms of purine nucleotide?
Mention the metabolic disorders associated with purine metabolism
7. Monoclonal antibodies.
8. PCR and its application.
9. Southern Blot techniques.
10. “Gilberts syndrome”
11. Acute intermittent porphyria.
*****
MBBS Phase – I Degree Examination - Dec-2014
Biochemistry – Paper I (RS2 & RS3)
Q.P. CODE: 1079
Draw neat, labeled diagrams wherever necessary
(Note: Both QP Codes 1079 and 1080 are to be, answered within total duration of three hours)
(Use separate Answer books for QP Code 1079 & 1080)

1. Describe the mechanisms of Blood Glucose regulation. What are the causes of Hyperglycaemia and
Hypoglycaemia?

2. What are the reactions of -oxidation of Palmitic acid? Give its Energetics.
3. What is the difference between Oxidative and Substrate level Phosphorylation? Give two examples
of Substrate level Phosphorylation.
4. Name three enzymes commonly estimated in Myocardial Infarction. Give its importance and
limitations.
5. Define Fatty Liver. What are the causes of Fatty Liver? Name the Lipotropic factors.
6. Describe the Digestion and Absorption of Proteins.

7. Mechanism of action of Steroid Hormones
8. Alkaptonuria
9. Eicosanoids – functions
10. Detoxification reaction – Phase I
11. Tertiary and quaternary structure of Proteins
*****
MBBS Phase – I Degree Examination - Dec-2014
Biochemistry – Paper II (RS2 & RS3)
Q.P. CODE: 1080

1. Define Replication. Describe in detail the process of replication in Eukaryotes.

2. Describe the catabolism of Heme in the body adding a note on clinical significance.
3. List the requirements, steps of Polymerase Chain reaction.
4. What is meant by Dietary Fiber? List the role of Dietary Fibers.
5. What are the causes of Respiratory Acidosis? List the primary abnormalities of Respiratory
Acidosis.
6. Name and explain the functions of plasma proteins with clinical significance.

7. Discuss the features of Lesch Nyhan syndrome.
8. Draw a neat labelled diagram of tRNA.
9. Tumour markers
10. What is meant by Renal Clearance? How is Creatinine Clearance calculated?
11. What are Restriction Enzymes? List three features of Restriction Enzymes.
*****
First Phase MBBS Degree Examination – <<>>

1. Describe the β-oxidation of fatty acids. Give its energetics and explain the regulation of acetyl
CoA in our body.

2. How is glycogen digested and absorbed? Describe glycogenolysis in the liver.
3. How are bile acid synthesized? Mention two functions of bile acids.
4. Describe the conversion of methionine to cysteine. Add a note on homocystinuria.
5. Outline the synthesis of epinephrine and give its functions.

6. Give the coenzyme role of pantothenic acid and its importance

7. Denaturation of proteins.
8. Uncouplers of oxidative phosphorylation.
9. Reverse cholesterol transport.
10. Bonds stabilizing protein structure.
11. UDP-Glucuronic acid.
*****
First Phase MBBS Degree Examination – JULY 2015

1. Draw neat diagram of Watson Crick model of DNA, explain its characteristics and the bonds that
play a role in the stability of DNA structure.

2. Describe salvage pathway of purine synthesis and its significance.
3. What are porphyrias? Mention four porphyrias with the defective enzyme.
4. Explain the role of kidneys in acid base regulation.
5. What is a balanced diet? Discuss the components of a balanced diet.

6. What are the sources of dietary fibers? Discuss the importance of it in nutrition. Outline the
functions of proteins.
7. Point mutation.
8. Hormones that regulate water balance
9. SDA.
10. Ribosomal RNA.
11. Define anti oxidants and give two examples.
*****
First Phase MBBS Degree Examination – DECEMBER 2015

1. Classify enzymes giving an example with the reaction catalysed.

2. Describe the digestion and absorption of lipids.
3. Discuss phenylketonuria under i) enzyme defect. ii) Manifestation. iii) Diagnostic test.
4. What are mucopolysaccharides. Give their importance with examples.
5. Coenzyme form of Vitamin B12 and its biochemical functions

6. Describe one carbon metabolism. What is its significance?

7. Compare and contrast Starch and Glycogen.
8. Essential fatty acids
9. Transport across cell membrane.
10. Melatonin.
11. Polyamines.
*****
First Phase MBBS Degree Examination – DECEMBER 2015

1. Write structure of DNA. Write a note on replication of DNA

2. What is the difference between endonuclease and restriction endonuclease? Give two examples
for endonuclease.
3. What are oncogenes? Discuss two tumor markers and their clinical application.
4. Diagnostic enzymes used in the assessment of different liver functions.
5. Respiratory alkalosis
6. How is uric acid formed in the body? What is Gout? What is the treatment? Explain the basis for
the treatment.
7. Serum electrophoresis.
8. Types of DNA probes
9. Hb as buffering agent.
10. Vitamin K functions and requirement
11. Point Mutation with 2 examples.
*****
MBBS Phase – I Degree Examination - JUNE 2016
Q.P. CODE: 1079

1. Give an account of Cholesterol biosynthesis with its regulation. Add a note on Atherosclerosis.

2. What are Uncouplers? Mention the Uncouplers of Oxidative Phosphorylation.
3. Describe Tryptophan metabolism.
4. Define Glycosaminoglycans. Describe its biomedical importance.
5. Isoenzymes
6. Describe Glycogenolysis. How it is regulated?

7. Biochemical changes in Starvation
8. Competitive inhibition of Enzyme activity
9. Rappaport Leubering cycle
10. Laboratory diagnosis for Hypothyroidism
11. Non-enzymatic Antioxidants
*****
MBBS Phase – I Degree Examination - JUNE 2016
Biochemistry – Paper II (RS2 & RS3)
Q.P. CODE: 1080

1. Describe the replication of DNA in Eukaryotes. Mention its inhibitors.

2. Recombinant DNA Technology and its applications.
3. What are Buffers? Explain the Plasma Buffers in maintaining Acid Base balance.
4. What is Methemoglobin? How it is formed? Mention the causes for Methemoglobinemia. How it is
detected?
5. What are Restriction Endonucleases? Give any two examples with their biomedical importance.
6. Describe how Bilirubin is metabolised in the body. Write the normal values of Serum bilirubin.

7. Balanced Diet
8. Reference values
9. Plasma proteins
10. Tests of Renal Distal Tubular function
11. Specific Dynamic Action
*****
MBBS Phase – I Degree Examination - DEC 2016
Q.P. CODE: 1079

1. Explain the effect of different factors on the rate of Enzyme Catalyzed reactions.

2. Define Gluconeogenesis. Explain the key reactions of Gluconeogenesis.
3. What are Essential Fatty Acids? What are the functions of Essential Fatty Acids?
4. Briefly discuss the Transamination reactions with examples.
5. -oxidation of Palmitic acid
6. Explain the synthesis of Catecholamines.

7. Explain the relationship between Km and Affinity.
8. What is meant by Denaturation of Proteins? What are the causes of Denaturation of Proteins?
9. Galactosemia
10. Discuss the role of Glutathione.
11. List the site inhibitors of Electron Transport Chain.
*****
First Phase MBBS Degree Examination – DEC 2016

1. Discuss RDA, Functions and Deficiency manifestations of Folic acid. How is it interlinked to
Vitamin B12?

2. Post translational modifications
3. Biochemical basis of Gout and its features
4. Recombinant DNA technology
5. Iron absorption and transport

6. Causes and general features of Porphyrias

7. Protein Energy Malnutrition
8. Marker enzymes of liver function test
9. Alkalosis
10. Diagnosis importance of serum protein electrophoresis
11. RNA polymerases
*****
MBBS Phase – I Degree Examination - AUG - 2017
BIOCHEMISTRY – PAPER I (RS2 & RS3)
Q.P. CODE: 1079

1. Describe the metabolism of Phenyl Alanine. Add a note on its inborn errors.

2. Glycogen storage disorders
3. Define Isoenzymes. Describe its biomedical importance citing any three examples.
4. Describe the Decarboxylation reactions of Amino acids with four examples. Give its significance.
5. Define Detoxification. Give any four reactions of Phase II Detoxification.
6. What is HMP Shunt? Give its significance.

7. Pellagra
8. Ketosis
9. Components of Electron Transport Chain
10. Hartnup’s disease
11. Lipoproteins
*****
First Phase MBBS Degree Examination – AUG - 2017

QP Code: 1080 – PAPER - II (Max.Marks:50)
(Use separate answer books for section A and Section B)

1. Discuss the process of protein biosynthesis. Name three inhibitors of protein biosynthesis.

2. Describe heme synthesis and add a note on its regulation.
3. Describe recombinant DNA-technology. Mention its applications.
4. Define biological value of protein. What do you mean by complementary proteins? Give
examples. What is the requirement of protein in diet?
5. Define codon. What are the salient features of a genetic code?
6. List any three trace elements with their biological function.

7. Mutagens.
8. Okazaki fragments.
9. Provitamins.
10. Cell cycle.
11. Tests to assess renal tubular function
*****
First Phase MBBS Degree Examination – OCT-2017
BIOCHEMISTRY - PAPER I (RS2 & RS3)

QP Code: 1079 (Max.Marks:50)
(Use separate answer books for section A and Section B)

1. Describe the reactions of glycolysis indicating the enzymes. Add a note on net yield of ATP under
aerobic and anaerobic conditions.

2. Describe the fate and formation of glycine. List four compounds formed from glycine.
3. What are isoenzymes? Explain the clinical significance giving two examples.
4. What are nitrogen-producing substances in the body? Explain how they are excreted from the
body.
5. Describe the fluid mosaic model of membrane structure.
6. Name the ring structure present in cholesterol. Write the key regulatory step in the synthesis of
cholesterol. Name four compounds derived from cholesterol.
7. Detoxification.
8. Chemiosmotic hypothesis.
9. Von Gierkes disease.
10. Multi enzyme complex.
11. Rappaport-Leubring cycle.
*****
MBBS Phase – I Degree Examination - OCT-2017
BIOCHEMISTRY – PAPER II (RS2 & RS3)

Q.P. CODE: 1080

1. What are the sources, functions, deficiency manifestations and daily-recommended allowance of
Thiamine?

2. Define Point Mutation. Explain the effects of Point Mutation.
3. Briefly explain the Lac Operon concept.
4. Discuss the features of Genetic Code.
5. Discuss the regulation of Water by Rennin-Angiotensin system.
6. What is Wilson’s disease? State the cause and the treatment policy.

7. Hypoalbuminemia
8. What are DNA probes? Mention the types of DNA probes.
9. Describe how Plasma Proteins are separated in the Clinical laboratory.
10. Discuss the nutritional role of Milk and Dairy products.
11. Discuss the role of Carbonic Anhydrase in the Acid Base regulation.
*****
MBBS Phase – I Degree Examination - JULY-2018
Q.P. CODE: 1079

1. Describe the formation, utilization and clinical significance of ketone bodies.

2. Amphibolic role of citric acid cycle
3. Pathway for synthesis of creatine, phosphocreatine and creatinine Clinical significance of creatinine
kinase
4. Outline the synthesis of cholesterol. Which is the key regulatory step
5. The IUBMB classification of enzymes with one example for each class
6. Different transport mechanisms across the cell membrane

7. Metabolic abnormality and clinical manifestation of galactosemia.
8. Three transmethylation reactions of S-adenosyl methionine
9. Regulation of glycolysis at the phosphofructokinase step
10. Energetics in the oxidation of one molecule of palmitic acid to carbon dioxide and water
11. Name three tumour markers and their clinical significance
*****
BIOCHEMISTRY – PAPER - II (RS2 & RS3)

Q.P. CODE: 1080

1. How is Uric acid formed from purine and add a note on Hyperuricemia.

2. Structure and function of tRNA
3. Vitamin A deficiency manifestations and it’s RDA
4. BMR
5. Erythrocytes in acid base balance
6. Heme biosynthesis

7. Role of selenium
8. Vandenberg test
9. Vectors in recombinant DNA technology
10. Types of immunoglobulin and their function
11. Acute intermittent Porphyria
*****
MBBS Phase – I Degree Examination - SEP-2018
QP Code: 1079

1. Describe how ammonia is formed and detoxified in the body.

2. Describe the various type of enzyme inhibition giving suitable examples.
3. Glycogenolysis
4. Define active transport. Explain the different types of active transport with suitable examples.
5. Significance of Hexose Mono Phosphate shunt pathway.

6. What are Xenobiotics? Give an account of phase two detoxification reactions

7. Biologically important compounds formed from glycine
8. Free radical scavenging systems
10. Pyruvate dehydrogenase complex
11. Oncogenes
*****
MBBS Phase – I Degree Examination - SEP-2018

Q.P. CODE: 1080

1. Explain the process of translation. Add a note on post translational modifications.

2. Biological functions and deficiency manifestations of Vitamin C
3. Role of plasma buffers in maintaining blood pH
4. BMR
5. Porphyrias
6. Polymerase Chain Reaction

7. Okazaki fragments
8. Gene therapy
9. Dietary fibres
10. Van den Bergh test
11. Acute phase proteins
*****

Q.P. CODE: 1079

1. Describe the Metabolism of phenylalanine and tyrosine and inborn errors associated with it.

2. Describe the steps of beta oxidation of fatty acids from palmitic acid to acetyl CoA.
3. Classify carbohydrates with two examples for each class and subclass.
4. Draw a labeled structure of cell with two organelles. Describe the functions of four organelles.
5. Fatty liver
6. Temperature and pH as factors affecting velocity of enzyme catalysed reactions, with examples

7. Fasting and glucose tolerance test criteria for diagnosis of diabetes mellitus
8. Specialized products formed from glycine
9. Anapleurotic reactions of citric acid cycle for three intermediates
10. Site specific inhibitors of electron transport chain with one example for each site
11. Phase two reactions of detoxification
*****

Q.P. CODE: 1080

1. Write in detail the process of translation in Eukaryotes. Add a note on post translational
modifications and its inhibitors.

2. Coenzymes of Cobalamin and its functions
3. Polymerase chain reaction
4. BMR
5. Porphyrias
6. Metabolic acidosis

7. Different types of RNA with their function
8. Scurvy
9. Reference values
10. Oncogenes
11. Gout.
*****
MBBS Phase – I Degree Examination - OCT-2019
QP Code: 1079

1. What is Gluconeogenesis? Write the steps involved in formation of Glucose from Alanine? Add a
note on its regulation.

2. Monosaccharides
3. Products from Arachidonic acid and their function
4. Conjugation in detoxification
5. Chemiosmotic theory of ATP formation

6. Digestion and absorption of lipids

7. Functions and markers for Lysosomes
8. Isoelectric pH
9. What are Coenzymes? Mention 3 with their functions.
10. Hyperglycemic hormones and their mode of action
11. Sphingolipids
*****
First Phase MBBS Degree Examination – OCT-2019

QP Code: 1080 – PAPER II

1. Explain the steps of initiation, elongation and termination of transcription. Add a note on post
transcriptional modification of RNA.

2. What is the primary defect in metabolic acidosis? List the causes of metabolic acidosis.
3. Name the different types of hemoglobin variants indicating their defects.
4. Name the protein energy malnutrition disorders. Write important differences between them.
5. Classify liver function tests. Describe the tests based on excretory functions.
6. How are purine nucleotide degraded? Mention the causes of hyperuricemia.

7. List the differences between RNA and DNA.
8. Mention the causes of orotic aciduria.
9. Explain the features of genetic code.
10. How is iron absorbed and transported. Add a note on hemochromatosis.
11. Write the causes and biochemical explanations for deficiency manifestations of vitamin B12.
*****
MBBS Phase – I Degree Examination - 28-Nov-2020
BIOCHEMISTRY – PAPER I (RS3)

QP Code: 1079

1. Name the aromatic amino acids. Discuss how phenylalanine is catabolised in the body. Add a
note on alkaptonuria.

2. Metabolism of high-density lipoprotein and its significance
3. Competitive and non-competitive enzyme inhibition with examples
4. How is galactose metabolized? Add a note on galactosemia.
5. Reactions of citric acid cycle (TCA cycle) and its energetics

6. Formation and utilization of Ketone bodies

7. Active transport across membranes
8. Application of radioactive isotopes in medicine
9. Significance of free radicals and antioxidants
10. Carcinogens
11. Enzyme linked immune sorbent assay
*****
MBBS Phase – I Degree Examination - 28-Nov-2020
BIOCHEMISTRY – PAPER II (RS3)

Q.P. CODE: 1080
Your answers should be specific to the questions asked.
Draw neat, labeled diagrams wherever necessary.

1. What is the normal range of blood pH? Discuss in detail the role of kidneys in pH regulation. Add a
note on metabolic acidosis.

2. Mutation
3. Polymerase Chain Reaction
4. Biochemical functions and deficiency manifestations of Vitamin A
5. Structure and functions of immunoglobulins

7. Biological role of copper in the body
8. Clearance tests
9. Protein energy malnutrition
10. Pellagra
11. Structure of tRNA
*****
MBBS Phase – I (CBME) Degree Examination - 17-Feb-2021
BIOCHEMISTRY – PAPER I (RS-4)

QP Code: 1024
(QP contains two pages)

1. Define lipoproteins? Mention the different lipoproteins involved in transport of lipids.
Explain metabolism of dietary lipids under the following heading.
a. Assembly of dietary lipids
b. Transport
c. Utilization in peripheral tissues
d. Metabolic fate [1+1+2+2+2+2]
2.1. A 12 year old girl presented with stiffness and tingling of hands and feet, carpopedal
spasm. On examination trousseau’s sign was positive, chvostek’s sign was positive. On
laboratory evaluation, serum calcium was significantly reduced.
a. Interpret the findings and suggest the probable diagnosis?
b. Mention the reference range and dietary sources of the nutrient.
c. Explain the role of hormones in regulating the blood levels of this nutrient.
d. Mention any 6 biochemical functions of this nutrient (1+2+4+3)

3. What are mucopolysaccharides?
a. Name the mucopolysaccharide present in the glomerular basement membrane.
What is its significance?
b. Explain the biochemical basis of heparin as anticoagulant.
c. Write the composition and importance of chondroitin sulphate?
d. Which mucopolysaccharide maintains the transparency of cornea? (1+1+1+1+1)
4. Define oxidative phosphorylation? Explain chemiosmotic hypothesis with a neat labelled

diagram. (1+2+2)
5. A 10 year old boy had difficulty in vision at night. However his vision was quite normal
during daytime except when he entered a dimly lit room. On investigation, his plasma
retinol levels were found to be low.
a. Suggest the probable diagnosis? Which nutrient deficiency causes this disease? (1)
b. Enumerate any four functions of the nutrient. (2)
c. Explain Walds visual cycle (2)
6. What is calorific value? Calculate the energy requirement of a 50 year old moderate
worker. (1+4)
7. Explain the effect of temperature and substrate concentration on enzyme activity with a
graph. (2+3)
8. Explain Fluid mosaic model of cell membrane with a neat labelled diagram.
Page 1 of 1
9. A 5 year old girl was brought to the hospital with enlarged abdomen. History revealed that
her childhood development was comparatively slow, frequently hungry, lethargic and
irritable. Clinical examination showed enlarged liver. Biochemical investigations of blood
sample revealed reduced fasting blood glucose levels and elevated levels of serum
lactate, triglyceride and uric acid
a. Suggest the probable diagnosis?
b. Name the enzyme defect?
c. What is the biochemical basis for fasting hypoglycemia, lactic acidosis and
hyperuricemia in this condition? (1+1+3 )
10. What is metabolic alkalosis? Mention four causes of metabolic alkalosis. Explain the
Compensatory mechanism. (1+2+2)
11. Explain the metabolic adaptations occurring in the liver and adipose tissue in a well-fed
state.
12. What are isoenzymes? Write the isoenzymes of CPK with tissue distribution. Which
isoenzyme is cardiac specific and write its pattern of rise in patients with myocardial
infarction. (1+2+1+2)

13. Explain the rationale behind using glycated hemoglobin (HbA1c) as an indicator of
glycemic control in diabetes mellitus. What is the reference range for HbA1c
14. Deficiency of lung surfactant causes Respiratory Distress Syndrome.

a. What is the composition of lung surfactant? (1)
b. What is the biochemical basis for Respiratory distress syndrome? (1)
c. What is the significance of L/S ratio (1)
15. Explain the structure of collagen. (5)
16. What is the coenzyme form of pyridoxine? Write two pyridoxine dependent reactions.
(1+2)
17. Mutual supplementation of cereals and pulses is beneficial. Justify. (3)
18. Give reason for the following:

a. Requirement of Thiamine is increased in Alcoholics (2)
b. Prescription of folic acid during early pregnancy (1)
19. Name the most effective physiological buffer in the plasma. Explain the role of carbonic
anhydrase in acid base homeostasis. (1+2)
20. Barbiturates should be given with caution in chronic alcoholics. Justify (3)
21. List routinely measured serum electrolytes. Mention their reference range. (1+2)
22. Write the type of inhibitions seen in the following :
a. Inhibition of Vitamin Kby Dicoumarol - an anticoagulant (1)
b. Inhibition of Cyclo-oxygenase by Aspirin. (1)
c. Inhibition of Placental Alkaline Phosphatase by Phenylalanine. (1)
*****
Page 1 of 2
BIOCHEMISTRY – PAPER II (RS-4)

Q.P. CODE: 1025
1. A 5 year old boy was brought to a Pediatrician with history of mousy odour of urine and
delay in achieving cognitive functions. On examination, the boy’s skin and hair was fair in
colour with hypopigmentation.
a. What is the probable diagnosis? (1)
b. Name the enzyme defect in the above disorder. (1)
c. Write the pathway for catabolism of the above amino acid (5)
d. Mention the reason for the cause of mousy odour in urine (1)
e. What biochemical tests are done to confirm the diagnosis? (2)
2. Describe the steps of transcription in prokaryotes. Mention the inhibitors of transcription.

Mention the post-transcriptional modifications. (6+1+3)

3. A 8 year old girl from endemic malaria area who had splenomegaly was investigated for
routine hematology, which revealed low hemoglobin of 7 gm%. Peripheral smear revealed
crescent shaped RBCs. She had no history of malaria attack.
a. What could be the molecular defect of hemoglobin in the above case? (2)
b. Name the biochemical investigations which can be done to confirm the diagnosis. (2)
c. Reason out why these patients show resistance to malaria. (1)
4. Interpret the following Liver Function Test report:
Total Direct Alkaline Ehrlich’s test Stool sample

Bilirubin bilirubin phosphatase
7.7 mg/dl 3.6 mg/dl 265 IU/L Negative Clay colour
a. What is the probable diagnosis? (1)

b. Mention the possible causes for the above condition? (2)
c. Substantiate with reasons for increase in conjugated fraction of bilirubin. (2)
5. Explain the steps in Polymerase Chain Reaction (PCR). Mention four applications of PCR.
(3+2)
6. Mention five tumor markers with their diagnostic importance.
7. Explain the disorders associated with purine synthesis and breakdown.
8. Describe the steps involved in heme degradation.
9. List the renal function tests. Explain the principle and application of creatinine clearance.
(2 +3)
Page 1 of 1
10 Explain structure and function relationship of protein with an example.
11 Explain the role of antioxidants in protection against reactive oxygen species (ROS).
12 Explain the immunological basis of vaccine development.

13. Explain the process of activation of proto-oncogenes to oncogenes.
14. Write the process of phase I detoxification with one example.
15. Name the polyamines and mention their clinical significance.
16. State the advantages of automation in clinical biochemistry laboratory.
17. Draw a neat labelled diagram of structure of t-RNA.
18. Mention the sources of carbon and nitrogen atoms of pyrimidine bases.
19. Mention the normal Albumin/Globulin (A/G) ratio. Give two disorders associated with
altered A/G ratio. (1+2)
20. Write the characteristics of genetic code.
21. Compare and contrast between nucleosides and nucleotides.
22. What are molecular scissors? Mention its applications. (1+2)
*****
Page 1 of 2
MBBS Phase – I Degree Examination - 31-Mar-2021

QP Code: 1079
1. Describe the pathway of glycolysis. How is it regulated? Add a not eon Rappaport – Leubering
cycle
2. Formation and utilization of Ketone Bodies
3. Absorption and transport of Iron
4. Biochemical role of Vitamin D
5. Classification of enzymes with examples
6. Compounds derived from Tyrosine
7. Functions of phospholipids
8. Inhibitors of electron transport chain
9. Biological active peptides
10. Lysosomes
11. Phase I reactions of biotransformation
*****
MBBS Phase – I Degree Examination – 31.03.2021

QP Code: 1080
Draw neat labeled diagrams wherever necessary.

1. Describe the sources, RDA, biochemical functions and deficiency manifestations of Vitamin A.

3. Biochemical changes and causes of metabolic alkalosis
4. Inhibitors of replication
5. Mutations
6. Use of serum enzyme markers and bilirubin as liver function tests

7. Basal metabolic rate
8. Reference value of serum albumin, A/G ratio and it clinical significance
9. Acute intermittent porphyrias
10. tRNA
11. Classes of immunoglobulins and their functions
*****
MBBS Phase – I (CBME) Degree Examination - 22-Jun-2021

QP Code: 1024
(QP contains three pages)

1.1. A 25 years old patient, known case of type 1 diabetes, was brought to casualty in
comatose state. History revealed that he was not taking insulin regularly. Biochemical
analysis of blood and urine showed the following findings.
Blood sugar -510mg/dl
Urine for Rothera’s test and Benedict’s test positive
Blood gas analysis report showed, pH -7.2, Bicarbonate-12mEq/L,
a. Suggest your probable diagnosis
b. Name the compounds which give Rothera’s test positive
c. Explain the principle of Rothera’s test
d. Explain the steps of synthesis utilization of these compounds (1+1+2+6)
2. a. Which Vitamin is called as sunshine vitamin?

b. What is its active form
c. How it is formed?
d. Write the biochemical functions and deficiency manifestations of this vitamin.
(1+1+4+4)

3. Define Anaplerosis. Describe any four anaplerotic reactions of citric acid cycle
intermediates. (1+4)
4. Define enzymes. Classify enzymes with one suitable reaction as an example for each class.
(1+4)
5. Draw a neatly labelled diagram of the complexes of the electron transport chain. Name
any two site specific inhibitors of each complex. (3+2)
6. What are dietary fibers? List any four and write their functions. (1+2+2)
7. A 13 year old girl complains of excessive tiredness, poor appetite and tingling sensation in
the limbs. On examination she was pale. Laboratory report revealed Hb-7gm/dl, TIBC is
increased, serum transfer in saturation is reduced and peripheral smear showed microcytic
hypochromic anemia.
b. Describe the absorption and transport of this nutrient. (1+4)
8. Draw a neat labelled diagram of a cell with the sub cellular organelles. Write the functions
of any four organelles. (3+2)
9. Write the formula to calculate anion gap; Mention its reference range. Discuss the clinical
use of anion gap in classifying metabolic acidosis with two examples for each type.
(1+1+3)
10. Name the urinary buffers. Explain their role in excreting excess acid from the body.
Mention the other renal mechanisms of pH homeostasis.
(1+2+2)
Page 1 of 1

11. What is the end product of aerobic glycolysis? Illustrate the fate of this compound. (1+2)
12. Write the diagnostic significance of each of the following enzymes.

a. Lipase b. Alanine amino transferase c. Creatine kinase (1+1+1)
13. Write the normal biological reference value for serum potassium. Mention any two causes
of hyperkalaemia. (1+2)
14. Name any four proteins of the Extracellular Matrix. Write the Posttranslational modification
of collagen and its importance. (1+2)
15. Name the mucopolysaccharide with anticoagulant activity. Write its composition and its
mechanism of action. (1+1+1)
16. Define nitrogen balance. Give one example each for conditions with positive and negative
nitrogen balance. (1+2)
17. Explain how long chain fatty acids are transported into the mitochondria. (3)
18. Give reason for the following

a. Muscle glycogen doesn’t contribute to blood glucose.
b. Intake of antimalarial drugs like Primaquin in some people causes haemolytic
anemia.
c. Humans cannot synthesize vitamin C (1+1+1)
19. Which vitamin deficiency is likely to develop in patients on Isoniazid, an antitubercular

drug? What is the co enzyme form of this vitamin? Write one biochemical reaction
dependent on this nutrient. (1+1+1)
20. What is the sorbitol pathway? Write the significance of sorbitol pathway. (1+2)
Multiple Choice Questions 10 x 1 = 10 Marks

21 i) Which one of the following subcellular organelle is involved in protein sorting
a. Lysosome
b. Golgi apparatus
c. Peroxisomes
d. Ribosames
21 ii) Ehlers-Danlos syndrome is due to the defective formation of -

a. Type I Collagen
b. Type II Collagen
c. Type III Collagen
d. Type IV Collagen
21 iii) Serum acid phosphatase enzyme level is increased in

a. Hepatic disease
b. Myocardial Infarction
c. Muscle disease
d. Prostate cancer
Page 1 of 2
21 iv) All are an example of Monosaccharide EXCEPT
a. Glucose
b. Galctose
c. Trehalose
d. Mannose
21 v) ___________ is the nitrogen containing phospholipid

a. Phosphatidylcholine
b. Phosphatidylinositol
c. Phosphatidylglycerol
d. Diphosphatidylglycerol
22 i) The site of action of Hormone sensitive lipase is in -

a. small intestine
b. capillary walls
c. mouth
d. adipocytes
22 ii) Glucose transporter 4 is the major glucose transporter in

a. RBC
b. neurons
c. adipose tissue
d. intestine
22 iii) ________________ is known to act as a physiological uncoupler

a. Valinomysin
b. Thyroxine
c. Carboxine
d. Oligomycin
22 iv) Which one of the lipoprotein fraction is elevated in hyperlipoproteinemia Type II A

a. VLDL
b. LDL
c. HDL
d. Chylomicrons
22 v) _____________ is the marker of Bone formation.
a. Telopeptides
b. Tartrate resistant acid phosphatase
c. Osteocalcin
d. Pyridinium cross links derived from collagen
******
Page 1 of 3
MBBS Phase – I (CBME) Degree Examination - 24-Jun-2021

Q.P. CODE: 1025
1.1. A 6 year old child was brought to the OPD with complaints of Mental retardation, delayed
developmental milestones, hyperactive and seizures. The child had light coloured hair,
skin and unpleasant mousy body odour. Serum Phenylalanine was 35mg/dl (Normal
1-2mg/dl). Ferric chloride test showed transient blue green colour in urine.
b. Mention the enzyme defect and write the reaction catalysed by their enzyme
c. Write the biochemical basis for the following clinical findings:
i. Neurological manifestations
ii. Light colouredhair and skin
iii. Mousy body odour
d. Describe the steps for synthesis of any two biological important compounds derived
from tyrosine. (1+2+3+4)
2.1. Explain in detail the reactions of Heme synthesis? Name the regulatory enzyme of this
pathway. How is it regulated? (6+1+3)

3.2. Classify amino acids based on their nutritional significance giving examples. What are non
protein amino acids? Give one example. (3+1+1)
3.
4.4. Mention any four anticancer drugs and write their mechanism of action. (1+4)
5.
5.6. A 40 year old male came with the complaints of difficulty in breathing, shortness of breath
and tightness of chest. History revealed that he is a chronic smoker for the past
15years.Chest X-ray and CT scan showed changes suggestive of emphysema.
a. Deficiency of which plasma protein causes this condition?
b. Explain the biochemical basis of emphysema in smokers?
c. Name any two serine proteases? (1+2+2)
7.
6. Explain the tests done to assess the renal tubular functions? What is urine osmolality?
Write its reference range? (3+1+1)
7. Name the RNA which carries amino acids to the site of protein biosynthesis. With
illustration explain the structure. (1+4)
8. A four year old child was brought to the hospital with the following complaints
developmental failure, aggressive behavior, joint pain, compulsive urge to bite his lips and
fingers. Mother revealed a family history of similar illness among family members.
a. Suggest the probable diagnosis.
b. Name an appropriate biochemical parameter to diagnose this condition and state its
reference range in males and females
c. Name the enzyme deficiency and the reaction catalysed by the enzyme (1+2+2)
9. Explain Lac operon concept with a diagrammatic representation.
10. Classify antioxidants giving two examples for each class.
Page 1 of 1
11. Telomerases are involved in aging process. Justify and give its clinical significance. (1+2)
12. What is Southern blot technique? Write two applications of this technique. (1+2)
13. Mention any three salient features of DNA replication. (3)
14. What is detoxification? Give two examples of conjugation phase reactions? (1+2)
15. What are DNA probes? Write their applications. (1+2)
16. What are oncosuppressor genes? Name any two with their mechanism of action. (1+2)

a. Restriction enzymes are termed as molecular scissors
b. Changing color of the bruise
c. Hemolytic jaundice is also called a acholuric jaundice (1+1+1)
18. Illustrate the sources of carbon and nitrogen atoms in Purine ring. (3)
19. Write the biochemical findings in the serum and urine in obstructive jaundice. (3)

a. Pellagra like symptoms are seen in Hartnups disease
b. Glycine does not exhibit optical activity
c. Proline is an α- helix breaker (1+1+1)

21 i) The protein part present in nucleoprotein is
a. Globin
b. Opsin
c. Histones
d. Apoferritin
21 ii) The enzyme defect in Acute intermittent porphyria

a. PBG- deaminase
b. UPG-cosynthase
c. Ferrochelatase
d. UPG-decarboxylase
21 iii) The following compounds are biosynthesized by Glycine EXCEPT

a. Creatinine
b. Heme
c. Melatonin
d. Purine nucleotide
21 iv) 5’-Nucleotidase is more specific for

a. Myocardial Infarction
b. Prostate cancer
c. Obstructive liver disease
d. Wilson’s disease
Page 1 of 2
21 v) Appearance Black colour urine is seen in
a. Porphyria
b. Alkaptonuria
c. Jaundice
d. Urinary tract infection
22 i) Which of the following has not been treated by gene therapy?

a. Hemophilia
b. Severe combined immunodeficiency
c. Cystic fibrosis
d. Glucose – 6- phosphatase deficiency
22 ii) Helicase enzyme in DNA replication -

a. Unwinds the DNA
b. releases the supercoils
c. breaks the strands
d. seals the strands
22 iii) Western blot technique is used for the

a. Detection of specific DNA segment
b. Detection of specific gene expression
c. Identification of a specific protein
d. Location of a gene on a specific chromosome
22 iv) Urine preservatives are used for all the following purposes EXCEPT
a. Reduce bacterial action
b. Minimize chemical decomposition
c. Increase pH
d. Decrease atmospheric oxidation of unstable compounds
22 v) Serum Alpha Fetoprotein level is increased in

a. Multiple Myeloma
b. Choriocarcinoma
c. Hepatoma
d. Lung cancer
******
Page 1 of 3
MBBS Phase – I Degree Examination - 30-Sep-2021

QP Code: 1079

1. What is the normal serum Cholesterol level? Explain the major steps of Cholesterol
biosynthesis. Add a note on Type II Hyperlipoproteinemia
2. Glycogenolysis and its regulation
3. Biochemical role of Vitamin B6
4. Diagnostic and therapeutic uses of enzymes
5. Factors regulating calcium Homoeostasis
6. Metabolism of Glycine and name the compound derived from it
7. Endoplasmic reticulum
8. Glucose – Alanine cycle
9. Maple syrup urine disease
11. Cytochrome P450
*****
MBBS Phase – I Degree Examination - 30-Sep-2021

Q.P. CODE: 1080

1. What is the normal blood pH? Discuss the various mechanisms by which the blood pH is
maintained.

2. Replication of DNA.
3. Regulation of blood calcium.
4. Biochemical functions and deficiency manifestations of Thiamine.
5. Genetic code.
6. Heme biosynthesis.

7. t-RNA.
8. Detoxification by conjugation
9. Reverse transcriptase
10. Fluorosis
11. Avidin.
*****
QP CODE : 1024
MBBS Phase – I (CBME) Degree Examination - 05-Mar-2022

QP Code: 1024

1. A 8 year old boy was brought to orthopaedic OPD with a complaint of abnormal gait for the
past 3 months. Clinical examination showed tenderness over Tibia.
Laboratory investigation data revealed
Investigation Patient report Normal range

Serum Calcium 8.2 mg/dl 8.6-10.5 mg/dl
Serum Phosphate 2.3 mg/dl 2.3-4.5 mg/dl
Serum Vitamin D 3 ng/ml 8-55 ng/ml
a. Name the vitamin D deficiency disorder in the above case
b. What is the RDA of vitamin D?
c. Explain the formation of calcitriol
d. Describe the role of calcitriol in calcium homeostasis
2. Explain glycogenolysis. Write the difference between Liver and Muscle glycogenolysis.
Mention the role of insulin and glucagon in glycogenolysis.

3. A pregnant lady who visited primary health care centre for antenatal check-up with
complaints of tiredness and easy fatigability was found to be anemic. Peripheral smear
showed microcytic hypochromic anemia.
a. Name the mineral associated with the above disorder
b. Write the dietary sources and RDA of the above mineral
c. Write the biochemical functions of above mineral.
4. A 60 year old obese man, who underwent master health check-up was found to have mild
hepatomegaly with fatty liver changes.
a. What is fatty liver?
b. Enumerate the causes of fatty liver
c. Explain the role of lipotropic factors in preventing fatty liver.
5. Mention blood buffers. Explain the role of Lungs in acid base balance.
6. List five functions of phosphorous.
7. Describe steps in Ketogenesis. Mention two conditions associated with Ketonuria.
8. What is chemiosmotic hypothesis? Explain how proton gradient is utilized for ATP
synthesis.
9. Describe competitive inhibition of enzymes with two examples.

10. Define Basal Metabolic Rate (BMR). Mention four factors affecting BMR.
Page 1 of 3
QP CODE : 1024
11. Mention three functions of cholesterol.
12. What is HbA1C (Glycated Hemoglobin)? Mention its significance.

13. What are therapeutic enzymes? Give two examples with their therapeutic application.
14. What is facilitated diffusion? Give one example.
15. What is the role of Anti Diuretic Hormone (ADH) in water balance? Name the disorder
associated with its deficiency.
16. What is Alkali reserve? List two causes of metabolic acidosis.
17. What is Marasmus? List two features of Marasmus.
18. Define Km. What is the significance of Km?
19. Name three mucopolysaccharides and write their functions.
20. Troponins are more specific cardiac marker compared to creatine kinase – Justify.

21 i) Galactosyl transferase is marker for
A. Cell membrane
B. Mitochondria
C. Lysosomes
D. Golgi complex
21 ii) Osteogenesis imperfecta is due to defect in:

A. Actin
B. Collagen
C. Keratin
D. Crystallin
21 iii) Bile acid is derived from

A. Cholesterol
B. Glycerol
C. Fatty acids
D. Billirubin
21 iv) Inulin is a polymer of

A. Glucose
B. Fructose
C. Mannose
D. Galactose
21 v) Which of the following mineral is best known for antioxidant role?

A. Calcium
B. Iron
C. Phosphorus
D. Selenium
22 i) Positive nitrogen balance is seen in

A. Pregnancy
Page 2 of 3
QP CODE : 1024
B. Malignancies
C. Malnutrition
D. Chronic illness
22 ii) Enzymes synthesized in inactive form is called as

A. Coenzymes
B. Apoenzymes
C. Proenzymes
D. Lysozymes
22 iii) Phospholipid deficiency in respiratory distress syndrome is

A. Sphingomyelin
B. Phosphatidyl ethanolamine
C. Plasmalogen
D. Lecithin
22 iv) Administration of loop diuretics leads to

A. Metabolic acidosis
B. Metabolic alkalosis
C. Respiratory acidosis
D. Respiratory alkalosis
22 v) Hyponatremia is seen in
A. Addison’s disease
B. Cushing’s disease
C. Primary hyperaldosteronism
D. Steroid therapy
******
Page 3 of 3
QP CODE : 1025
MBBS Phase – I (CBME) Degree Examination - 08-Mar-2022

Q.P. CODE: 1025
1. A child of two years presented with convulsions. He was taking normal feeds. But his
mother observed mousy odour of child’s urine. Urine ferric chloride test was positive.
Plasma phenylalanine was found to be elevated. He was diagnosed to have phenyl
Ketonuria
a) What is the biochemical defect in phenyl Ketonuria?
b) Describe the catabolism of phenylalanine
c) Give the biochemical reasons for mousy odour in this case
2. Describe protein biosynthesis in prokaryotes. Mention three inhibitors of protein

biosynthesis

3. A 45 year old man presented with severe back pain and weakness. He had lost 7 kgs in last
three months. He complained of loss of appetite and fatigue. X-ray showed punched out
lesions. Urine is positive for Bence Jones protein
a) Name the disorder in above case
b) What are Bence Jones proteins?
c) What is the electrophoretic pattern that is observed in this case?
1.
4. A known case of diabetes and hypertension on irregular treatment presented with swelling
of both lower limbs and puffiness of face. He was diagnosed with chronic kidney disease
(CKD)
a) Mention two biochemical parameters altered in CKD.
b) Explain the test to assess glomerular function of Kidney.
5.2. What is Porphyria? Write the types of porphyria. Mention enzyme defect and clinical features
of acute intermittent porphyria
3.
6. How are free radicals generated? Describe the free radical scavenging systems
7. List the hormones which function with cAMP as second messenger. Describe the mechanism
of action of steroid hormones
8. Enumerate the reactions of purine salvage pathway. Name the disorders that is associated
with this pathway and write its clinical features
9. What are restriction endonucleases? Give two examples. Explain their role in Recombinant
DNA technology
10. What is polymerase chain reaction (PCR)? Explain the steps in PCR. Write two applications
of PCR
Page 1 of 3
QP CODE : 1025
11. List out the assays done for evaluation of thyroid function. Enumerate the laboratory
findings in hyperthyroidism
12. What is detoxification? Give two examples of detoxification by oxidative reaction
13. What are reference intervals? List out two pre analytical variables
14. What is Southern Blotting Technique? Mention its applications
15. Name three nucleotides and write their biological importance
16. What is innate and adaptive immune response?
17. Give three examples of tumour markers and write their clinical importance
18. Write the serum and urinary biochemical findings in hemolytic jaundice
19. What are oncogenes? What are the factors that activate oncogenes?
20. What are essential amino acids? Give examples

21 i) Heme is converted to bilirubin in
A. Mitochondria
B. Microsomes
C. Golgi apparatus
D. Plasma membrane
21 ii) Immunoglobulin which crosses placenta is

A. IgG
B. IgA
C. IgM
D. IgD
21 iii) The amino acid which do not allow formation of alpha helix is
A. Glutamate
B. Proline
C. Tyrosine
D. Histidine
21 iv) Histones are rich in

A. Glutamic acid and aspartic acid
B. Glycine and serine
C. Methionine and cysteine
D. Arginine and Histidine
21 v) Which of the following is a termination codon?

A. AAG
B. CAG
C. CAA
D. UAG
22 i) In which of the following phase of cell cycle DNA replication takes place
A. G1
B. G2
C. S
Page 2 of 3
QP CODE : 1025
D. M
22 ii) Which of the following antioxidant enzyme is selenium dependent?

A. Glutathione peroxidase
B. Glutathione reductase
C. NADPH oxidase
D. Catalase
22 iii) Which of the following compound used in the treatment of gout is a competitive inhibitor
of xanthine oxidase?
A. Probenicid
B. Allopurinol
C. Colchicine
D. Acetaminophen
22 iv) Normal serum level of albumin is

A. 1.5 to 2.5 gm/dl
B. 3.5 to 5 gm /dl
C. 6 to 7.5 gm/dl
D. 9 to 11 gm/dl
22 v) End product of catabolism of protein is?

A. Urea
B. Uric acid
C. Creatinine
D. Orotic acid
******
Page 3 of 3
MBBS Phase – I Degree Examination - 05-Mar-2022

QP Code: 1079

1. Explain in detail the beta oxidation of palmitic acid. Add a note on its energetics.

2. Classification of enzymes with examples.
3. Digestion and absorption of carbohydrates
4. Metabolic functions of glycine
5. Hormonal regulation of blood glucose

6. Urea cycle

8. Specificity of enzymes
9. Structure and functions of mitochondria
10. Tumour markers
11. Fatty liver
*****
MBBS Phase – I Degree Examination – 05-Mar-2022

Q.P. CODE: 1080

1. Write in detail about heme synthesis and its regulation. Add a note on Acute intermittent
porphyria

2. Purine catabolism and its disorder
3. Role of protein buffers in acid-based balance
4. Biological value of proteins
5. Antioxidants
6. Glomerular function test

7. Gene therapy
8. Specific Dynamic Action (SDA)
9. Anion gap
10. Messenger RNA
11. Posttranscriptional modifications
*****
QP CODE : 1024
MBBS Phase – I (CBME) Degree Examination - 05-May-2022

QP Code: 1024
1. A 10-year-old boy with poor nutritional intake was brought to the ophthalmology OPD with
history of difficulty in vision in dim light. Incidentally, on examination, he had few lesions
on skin. A provisional diagnosis of vitamin deficiency was made.
(a) Name the fat-soluble vitamin deficiency associated with the above case.
(b) Write the recommended dietary allowance (RDA) for above vitamin.
(c) Explain Wald’s visual cycle.
(d) Write any two other functions of this vitamin.
2. Write the steps in beta-oxidation of palmitic acid. Explain the energetics of the pathway.
3. A known diabetic patient on regular insulin treatment was brought to the casualty in a
semi-comatose state. He had history of vomiting and diarrhea for the past two days and
his food intake was reduced. His random blood sugar (RBS) on admission was 45mg/dl.
(a) Interpret the glucose value in the above case.
(b) Explain hormonal regulation of blood glucose level.
4. An elderly patient with history of chronic smoking presented to medicine OPD with history
of difficulty in breathing. Following respiratory system examination, physician made a
diagnosis of chronic obstructive airway disease and his arterial blood was sent for arterial
blood gas (ABG) analysis.
(a) Write the probable acid-base disorder in the above condition.
(b) Mention the compensatory mechanisms for the above acid-base disorder.
(c) Write the biological reference interval for:
(i) Blood pH (ii) Blood pCO2 (iii) Plasma bicarbonate
5. Classify enzymes and give one example to each class.
6. Explain the components of electron transport chain.
7. Mention the significance of gluconeogenesis. Write the reactions catalyzed by the key
enzymes of gluconeogenesis.
8. Mention the biological reference interval for serum sodium. Write any three biochemical
functions of sodium. List two causes for hyponatremia.
9. Explain five factors affecting basal metabolic rate (BMR).
10. Explain the regulation of serum calcium level.
Page 1 of 3
QP CODE : 1024
11. Define respiratory quotient (RQ). Mention the RQ for carbohydrate. Name one condition
responsible for decrease in RQ.
12. Explain uniport, symport and antiport transport system with one example for each.
13. Name any three mucopolysaccharides and write their biological importance.
14. Name three therapeutic enzymes and write their uses.
15. Name essential fatty acids. Mention two functions of essential fatty acids.
16. Mention the metabolic pathways in Liver that are activated during starvation.
17. Write the biochemical functions of iodine. Mention the disorder associated with iodine
deficiency.
18. What is anion gap? Write two conditions associated with high anion gap acidosis.
19. Name three enzyme profile in liver diseases and mention their diagnostic significance.
20. What is leptin? Mention its biological importance.

21 i) Which one of the following enzymes is present in lysosomes?
A. Phospholipase
B. Aldolase
C. Acetyl CoA carboxylase
D. HMG CoA reductase
21 ii) Which one of the following is a noncompetitive inhibitor?

A. Allopurinol
B. Iodoacetate
C. Methotrexate
D. Lovastatin
21 iii) Which one of the following is a dietary fibre?

A. Starch
B. Heparin
C. Pectin
D. Dextrin
21 iv) Which one of the following is involved in the formation of liposomes?

A. Lipoproteins
B. Triglyceride
C. Free cholesterol
D. Phospholipids
Page 2 of 3
QP CODE : 1024
21 v) Which one of the following is an allosteric inhibitor of phosphofructokinase?
A. Fructose-6-phosphate
B. Fructose-2, 6 bisphosphate
C. AMP
D. Citrate
22 i) Lipoprotein lipase is activated by

A. Apo A-I
B. Apo B 100
C. Apo E
D. Apo C – II
22 ii) Which one of the following is a feature of Ehlers-Danlos syndrome?

A. Loose skin
B. Poor wound healing
C. Ectopia lentis
D. Brittle bones
22 iii) The daily requirement of vitamin D in adult males is

A. 10 microgram
B. 20 microgram
C. 30 microgram
D. 40 microgram
22 iv) Which one of the following mineral is present in Vitamin B12?

A. Calcium
B. Cobalt
C. Chromium
D. Copper
22 v) An example for cardiac glycoside is

A. Digitalis
B. Sorbitol
C. Glucuronic acid
D. Mannosamine
******
Page 3 of 3
QP CODE : 1025

Q.P. CODE: 1025
1. A 50 year old obese man with history of alcoholism presented with acute pain and swelling
of the great toe. His laboratory investigations revealed serum uric acid level of 10mg/dl. A
diagnosis of gout was made and further evaluation was suggested.
(a) Explain the steps in the formation of uric acid.
(b) Mention the causes of primary and secondary gout.
(c) Write the basis for treatment of gout with the drug allopurinol.
2. Enumerate the steps in recombinant DNA technology. Explain the role of vectors used in
recombinant DNA technology. Write two medical applications of recombinant DNA
technology.
3. A 60 year old man who is a known case of diabetes mellitus and hypertension presented
with passing frothy urine, nausea and hiccups. Following biochemical investigations, blood
urea and serum creatinine were elevated and a diagnosis of chronic kidney disease (CKD)
was made.
(a) Where is urea formed in the body?
(b) Mention the biological reference interval for blood urea.
(c) Mention one pre-renal, renal and post-renal cause for increase in blood urea level.
4.1. A young patient who presented with fever, nausea, vomiting and yellowish discoloration of
eyes was diagnosed to be suffering from viral hepatitis.
(a) Write the serum and urine biochemical findings in a case of hepatic jaundice.
(b) Write the type van den Bergh reaction seen in above case.
5.2. Name five tumor markers and write their diagnostic significance.
6. Explain the role of antioxidants in prevention of free radical injury.
7. Explain the steps of DNA replication in prokaryotes.
8. Explain the structure and functions of DNA.
9. Name five plasma proteins and write their functions.
10. Enumerate the biologically important compounds formed from glycine. Write their
significance.
Page 1 of 3
QP CODE : 1025
11. Name the essential amino acids and write their significance.
12. Name three immunoglobulins and write their functions.
13. Name three variables leading to pre-analytical errors in clinical laboratory.
14. What is Western blotting technique? Write its applications.
15. Write three features of genetic code.
16. Enumerate three Transmethylation reactions.

17. Enumerate three examples for post-translational modification of proteins.
18. What are porphyrias? Write the enzyme defects of any two porphyrias.
19. Write the mechanism of action of steroid hormones.
20. Name three compounds formed from tryptophan and write their significance.

21 i) Which one of the following is a peptide?
A. Collagen
B. Hemoglobin
C. Myoglobin
D. Inulin
21 ii) N- Acetyl glutamate (NAG) regulates which of the following urea cycle enzymes?
A. Carbamoyl phosphate synthetase I
B. Ornithine transcarbamoylase
C. Argininosuccinate synthetase
D. Arginase
21 iii) Bence Jones protein is seen in

A. Hepatoma
B. Multiple myeloma
C. Ovarian cancer
D. Colon cancer
21 iv) Which one of the plasma protein is decreased in patients with nephrotic syndrome?
A. Albumin
B. Immunoglobulin
C. Alpha2 macroglobulin
D. Beta globulins
21 v) In which hemoglobin iron is present in ferric state?

A. Sulfhemoglobin
B. Carboxyhemoglobin
C. Methemoglobin
D. Sickle cell hemoglobin
22 i) The conjugating agent for bilirubin is

A. Glycine
B. Cysteine
C. Glutamine
D. Glucuronate
Page 2 of 3
QP CODE : 1025
22 ii) During DNA replication, supercoiling is removed by
A. Polymerase
B. Topoisomerase
C. Helicase
D. Ligase
22 iii) Which of the following enzyme is elevated in obstructive jaundice?

A. Alkaline phosphatase
B. Neuron specific enolase
C. Acid phosphatase
D. Lipoprotein lipase
22 iv) Sugar present in RNA is

A. Ribose
B. Ribulose
C. Deoxyribose
D. Xylose
22 v) The closeness of the result of a quality control to its true value is termed as
A. Sensitivity
B. Specificity
C. Accuracy
D. Precision
******
Page 3 of 3
MBBS Phase – I Degree Examination - 05-May-2022

QP Code: 1079

1. Write the steps of β-oxidation of palmitic acid. Add a note on energetics.
2. Formation and utilization of ketone bodes.
3. Urea cycle.
4. Homopolysaccharides.
5. Substrate level Phosphorylation
6. Isoenzymes
7. Biochemical function and markers of Mitochondria
8. Lactose intolerance.
9. Anapleurotic reactions
10. Markers of carcinoma prostate
11. Essential fatty acids.
*****
MBBS Phase – I Degree Examination - 05-May-2022

QP Code: 1080

1. What is normal pH of blood? Discuss in detail role of kidneys in pH regulation. Add a note
on metabolic acidosis.

2. Biochemical functions, recommended dietary allowance and the deficiency of thiamine
3. Mutation
4. Dietary fibre.
5. Salvage pathway of purine nucleotides with the clinical disorders associated with it.
6. Outline the degradation of heme and excretion of products of degradation

7. Bile salts and bile pigments in the diagnosis of various types jaundice
8. Oncogene.
9. Orotic aciduria
10. Functions of albumin.
11. Clearance test.
*****
First Phase MBBS Degree Examination – 08-Aug-2022

QP Code: 1079

1. Describe the β-oxidation of saturated fatty acids. Explain the role of co-enzymes and write the
energetics of complete oxidation of Palmitic acid.
2. Write the role of kidney in maintaining acid base balance.
3. Describe the composition and importance of Glycosaminoglycans.
4. Urea cycle.
5. What is the normal cholesterol level? Name the products synthesis from cholesterol. Mention the
pathological causes of hypercholesterolemia.
6. What is oxidative phosphorylation? Explain the Chemi-osmotic theory.
7. Explain the fluid mosaic model of membrane structure.
8. What is glycated hemoglobin? Mention its normal level. What is its significance?
9. What are coenzymes? Give examples. Write their importance.
10. What are uncouplers? Give examples.
11. Lactose intolerance.
*****
MBBS Phase – I Degree Examination - 08-Aug-2022

Q.P. CODE: 1080

1. Write in detail the sources requirement, Biochemical functions of and deficiency manifestations of
Vitamin –D.

2. Glomerular function tests
3. Role of Lungs in acid base balance
4. Different types of Jaundice with their biochemical abnormalities and tests to evaluate them
5. BMR
6. Dietary fibers

7. Wilson’s disease
8. Anti diuretic hormone
9. Oncogene.
10. Sickle cell anaemia
*****
QP CODE : 1024

QP Code: 1024

1. A medical student who had an exam on the next day did not eat anything the previous
night. Next day morning, he had severe headache and giddiness before exam. His fasting
plasma glucose was 48 mg/dl.
a) Interpret the plasma glucose value
b) Name the metabolic pathways which maintain blood glucose in fasting state
c) Explain the metabolic pathway that synthesise glucose from pyruvate
2. Mention the active form of Vitamin D. Describe the synthesis, biochemical functions and
RDA of Vitamin D.

3. A 48-year-old man diagnosed with myocardial infarction (MI) had an altered lipid profile with
elevated total cholesterol and LDL cholesterol.
a) Write the biological reference interval of LDL cholesterol.
b) Explain the formation of LDL cholesterol.
c) Reason out why LDL cholesterol is atherogenic.
4. A 70-year-old man suffered an attack of pneumonia. He found it difficult to breathe and was
losing consciousness. His Arterial Blood Gas (ABG) report was as follows: pH=7.1, pCO2 =
52 mmHg, Plasma Bicarbonate (HCO3-) = 25 meq/L.
a) Interpret the ABG report.
b) Write the compensatory mechanism in the above acid-base disorder.
5. Mention biological reference interval for serum calcium. Describe any four functions of
calcium.
6. Define Isoenzymes. Mention the Isoenzymes of creatine phosphokinase (CPK) and write their
significance.
7. Define Basal Metabolic Rate (BMR). Enumerate the factors affecting BMR.
8. Explain the metabolic adaptations in well-fed state.
9. Explain competitive inhibition of enzymes with two examples.
10. Explain the functions of peroxisomes and describe their role in fatty acid oxidation.
11. What is fatty liver? Mention any two lipotropic factors.
12. What is hyponatremia? List two causes of hyponatremia.
13. Component of oral rehydration solution (ORS) has sodium chloride and glucose. What is
purpose of adding glucose in ORS?
14. Mention any three site specific inhibitors of electron transport chain.
15. Name the enzyme defect in von Gierke’s disease. Write the biochemical alterations in von
Gierke’s disease.
16. What is the cause of pellagra? Write the clinical manifestations of pellagra.
17. A diabetic patient was advised not to take polished rice but to take brown rice. Explain the
reasons for the same.
18. Mention three homopolysccharides of glucose and write their biological importance.
19. Write the biochemical defect in Ehler Danlos Syndrome and Osteogenesis imperfecta.
20. Write the biochemical cause of respiratory distress syndrome in premature babies.
Page 1 of 3
QP CODE : 1024
21 i) Hexokinase belongs to which class of enzymes?
A. Oxidoreductase
B. Transferase
C. Hydrolase
D. Lyase
21 ii) Which of the following vitamins is used in the electron transport chain?
A. Riboflavin
B. Pantothenic acid
C. Pyridoxine
D. Biotin
21 iii) Glucose and fructose are monosaccharide units of

A. Lactose
B. Maltose
C. Sucrose
D. Isomaltose
21 iv) The sugar component of cerebroside is

A. Galactose
B. Lactose
C. Fructose
D. Ribose
21 v) The normal Anion gap is

A. 4-8 mmol/L
B. 10-14 mmol/L
C. 16-20 mmol/L
D. 22-26 mmol/L
22 i) Limiting amino acid in the protein gelatin is

A. Lysine
B. Threonine
C. Tryptophan
D. Methionine
22 ii) Which coenzyme is responsible for carboxylation reactions

A. Biocytin
B. FAD
C. NAD
D. TPP
22 iii) Hormone insulin activates which of the following pathway

A. Glycogenolysis
B. Gluconeogenesis
C. Glycolysis
D. Lipolysis
22 iv) In Wilson’s disease copper accumulates in all of the following tissues EXCEPT
A. Eyes
B. Spleen
C. Brain
D. Liver
22 v) The marker enzyme for microsomes is

A. ATP synthase
Page 2 of 3
QP CODE : 1024
B. Cathepsin
C. Glucose-6-phosphatase
D. Lactate dehydrogenase
*****
Page 3 of 3
QP CODE : 1025

Q.P. CODE: 1025
1. A 10 year old boy was brought to the hospital for self-multilating behaviour and delayed
development. His serum uric acid level was 15 mg/dl. A provisional diagnosis of Lesch Nyhan
syndrome was made.
a) Write the biological reference interval for serum uric acid level.
b) Name the enzyme defect and the pathway affected in the above disorder.
c) Which tissues are dependent on this pathway?
d) Enumerate the other causes of hyperuricemia
e) What is the role of allopurinol in the treatment of hyperuricemia?
2. Describe the steps of DNA replication in prokaryotes. List the difference between
prokaryotic and eukaryotic DNA replication.
3.a) A 15 year old tribal boy was admitted with complaints of fatigue, recurrent fever and pain in
arms and legs. His peripheral blood smear shows sickled erythrocytes and a hemoglobin
concentration of 6 gm%.
a) Name the molecular defect in this disorder.
b) Explain the mechanism of sickling.
c) What is the cause of anemia in this condition?
4.d) An intravenous drug user was found to have developed jaundice. Laboratory investigations
revealed hepatitis B infection. His total serum bilirubin was 10.2 mg/dl.
a) What type of jaundice is seen in above case?
b) Explain van den Bergh test and write its interpretation in the above case.
5. Describe the steps in this polymerase chain reaction (PCR). Name the type of PCR used in
the diagnosis of Covid 19.
6. Name any three products derived from tyrosine. Describe the metabolic pathway leading to
the formation of any one of the product from tyrosine.
7. Draw the structure of immunoglobulin G and label it. Enumerate its functions.
8. What is lipid peroxidation? Explain the role of antioxidants in scavenging reactive oxygen
species.
9. Write the steps in the formation of creatine and glutathione from glycine.
10. Describe the glomerular function tests.
Page 1 of 3
QP CODE : 1025
11. Name three tumor markers and mention their significance.
12. What is the enzyme defect in maple syrup urine disease? What are its characteristic
features?
13. List the adrenal function tests. Mention one disorder associated with abnormal adrenal
function.
14. Enlist three biologically important peptides and write their functions.
15. What are xenobiotics? Write two detoxification reactions by conjugation.
16. Name three biologically important nucleotides and mention their importance.
17. Mention three advantages of automation in clinical biochemistry laboratory.
18. Enlist three post-translational modifications with suitable examples.
19. Mention normal albumin/globulin (A/G) ratio. Write two conditions where A/G ratio is
altered.
20. What is restriction fragment length polymorphism (RFLP). Mention two clinical applications
of RFLP.

21 i) All the following are glucogenic amino acids EXCEPT
A. Valine
B. Phenylalanine
C. Glycine
D. Leucine
21 ii) N3 of purine ring is donated by

A. Asparate
B. Glycine
C. Glutamine
D. Ammonia
21 iii) Which of the following enzymes is responsible for immortality of cancer cells?
A. Telomerase
B. RNA polymerase I
C. DNA polymerase
D. Helicase
21 iv) In which of the following conditions is serum direct bilirubin elevated

A. Physiological jaundice in the newborn
B. Crigler – Najjar syndrome
C. Gilbert’s syndrome
D. Gall stones
21 v) Enzyme defect in acute intermittent porphyria is

A. ALA synthase
B. ALA dehydratase
C. PBG deaminase
D. Uroporphyrinogen decarboxylase
Page 2 of 3
QP CODE : 1025
22 i) Closeness of a result to the true value is termed as
A. Precision
B. Accuracy
C. Sensitivity
D. Specificity
22 ii) Reference interval for pH of urine is

A. 3.5 to 4.5
B. 5.5 to 6.5
C. 7.5 to 8.5
D. 9.5 to 10.5
22 iii) Southern blotting technique is used for detection of

A. DNA
B. RNA
C. Protein
D. Lipoprotein
22 iv) Which of the following is an example for acute phase protein?

A. Prothrombin
B. C-reactive protein
C. Lipoprotein A
D. Thyroxine binding globulin (TBG)
22 v) Epidermal growth factor (EGF) is produced by

A. Platelets
B. Monocytes
C. Endothelial cells
D. Fibroblasts
******
Page 3 of 3
MBBS Phase – I Degree Examination - 14-Feb-2023

QP Code: 1079

1. Define Gluconeogenesis. Name the substrates required for Gluconeogenesis and trace the
pathway for formation of glucose from lactate. Add a note on regulation of
Gluconeogenesis.
2. Inborn errors associated with phenyl alanine and Tyrosine metabolism.
3. Classify enzymes with examples.
4. Urea cycle.
5. Name the ketone bodies. Describe the formation and utilization of ketone bodies.
6. Biomarkers for early detection of acute myocardial infarction.
7. Enzymes of therapeutic importance.
8. HDL metabolism.
9. Primary structure of proteins.
10. Name three tumour markers and their clinical significance.
11. Antioxidants.
*****
MBBS Phase – I Degree Examination - 14-Feb-2023

Q.P. CODE: 1080

1. Define transcription. Explain in detail the transcription in Prokaryotes. Add a note on a note on
post transcriptional modifications.

2. Dietary Fibers
3. Salvage pathway of purines
4. List the body fluid buffers and discuss their role in regulation of blood pH.
5. Immunoglobulins.
6. Lac operon concept

7. Oncogenes.
8. Lesch Nyhan syndrome.
9. Okazaki fragments
10. Creatinine clearance
11. Acute intermittent porphyria
*****
QP CODE : 1024

QP Code: 1024

1. A 10-year-old boy was admitted to a hospital with a diagnosis of malaria. He was started
on primaquine and antipyretics. Within one day he was found to have developed
hemolytic anemia.
a) Name the pathway affected in the above case and write the enzyme defect in the
pathway.
b) Name the compounds formed in this pathway and write their importance.
c) What is the relation between primaquine and hemolytic anemia?
2. Describe cholesterol biosynthesis up to the formation of mevalonate. Explain the
regulation of cholesterol biosynthesis. Mention two causes of Hypercholesterolemia.

3. An 8-year-old girl presented with difficulty in vision during night time. Vitamin A
deficiency was suspected following examination.
a) Write the provitamin form of Vitamin A
b) Explain Wald’s visual cycle
4. A 20-year-old pregnant woman presented with history of fatigue. Her peripheral blood
smear showed microcytic hypochromic anemia.
a) Which mineral deficiency leads to this type of anemia?
b) Explain the absorption, transport and storage of this mineral.
5. Describe the role of dietary fibre in nutrition.
6. State chemiosmotic theory and illustrate the process of oxidative phosphorylation.
7. Define metabolic acidosis. Enumerate the causes for metabolic acidosis. Write the
compensatory mechanism in metabolic acidosis.
8. Describe the role of any five plasma enzymes in the diagnosis of disease.
9. Explain niacin under the following headings:
a) Dietary sources
b) Co-enzyme forms
c) Deficiency manifestation
10. Explain the metabolic changes in starvation.

11. Write the composition and functions of collagen.
12. Enumerate the biomarkers used in the diagnosis of myocardial infarction (MI). Which
biomarker is considered specific for MI and why?
13. Name three functions of the vitamin whose deficiency causes scurvy.
14. Name three mucopolysaccharides and write their functions.
15. Name three phospholipids and write their biological importance.
16. Mention two causes of hypokalemia. Write biological reference interval for serum potassium.
17. Define Km. Explain its importance with an example.
18. Mention the role of carnitine in β-oxidation.
19. Write biological importance of selenium.
20. Define active transport. Give two examples for active transport.
Page 1 of 3
QP CODE : 1024
21 i) All the following lipids are present in the cell membranes EXCEPT
A. Lecithin
B. Cholesterol
C. Sphingomyelin
D. Triacylglycerol
21 ii) Which of the following derivative of monosaccharide is used to reduce raised intra-cranial
pressure?
A. Sorbitol
B. Dulcitol
C. Ribitol
D. Mannitol
21 iii) Enzymes which are synthesized in an inactive form are called
A. Apoenzyme
B. Proenzymes
C. Coenzyme
D. Isozyme
21 iv) The product of glycolysis in erythrocytes is

A. Lactate
B. Pyruvate
C. Urate
D. Acetate
21 v) The vitamin that acts as a coenzyme for transketolase activity is

A. Pyridoxine
B. Thiamine
C. Biotin
D. Folate
22 i) Normal biological reference interval for serum sodium is
A. 96-105 meq/L
B. 116-135 meq/L
C. 136-145 meq/L
D. 156-165 meq/L
22 ii) Number of calories given by one gram of carbohydrate is
A. 2
B. 4
C. 6
D. 9
22 iii) Nitrogenous base ethanolamine is present in
A. Phosphatidyl inositol
B. Plasmalogen
C. Cephalin
D. Lecithin
22 iv) The ratio of bicarbonate to carbonic acid in bicarbonate buffer system is
A. 20:1
B. 10:1
C. 4:1
D. 1:1
22 v) Which of the following does not increase the absorption of calcium?

A. Vitamin D
B. Absence of bile salts
C. Basic amino acids
D. Acidity
Page 2 of 3
QP CODE : 1024
*****
Page 3 of 3
QP CODE : 1025

Q.P. CODE: 1025
1. A patient who was suffering with pain abdomen and passing clay coloured stools came to
medical OPD for treatment. On examination there was yellowish discoloration of sclera.
Following investigations a diagnosis of obstructive jaundice was made.
a. Explain the formation and fate of bilirubin
b. Name two causes of obstructive jaundice
c. Write the serum and urinary findings in obstructive jaundice
2. What is semiconservative replication? In which phase of cell cycle replication takes place?
Describe replication in prokaryotes with neatly labelled diagram.

3. A 7 year old boy presented with oedema and passing frothy urine. Investigation revealed
severe proteinuria.
a. What is the normal plasma level of total proteins and albumin?
b. Name two other disorders associated with hypoalbuminemia
c. Mention the functions of albumin.
4. A child was rushed to the emergency ward with altered sensorium. On examination, the
child was found to be in semi comatose stage. Investigations revealed high blood ammonia
levels and the case was suspected to be urea cycle disorder.
a. Explain urea cycle
b. Mention any two disorders of urea cycle with its enzyme defect
5. Explain tertiary structure of proteins. List the forces maintaining tertiary structure.
6. What is polymerase chain reaction (PCR)? Describe the steps involved in PCR.
7. Enumerate five transmethylation reactions and mention their significance.
8. Describe the structure of immunoglobulins. Name any two classes of immunoglobulins and
write their functions.
9. What are nucleotides? Name any four biological important nucleotides and write their
importance.
10. List various reactive oxygen species. Describe the damages produced by reactive oxygen
species.

11. Name blotting techniques. Write the applications of each technique.
12. Draw purine ring and indicate the sources of carbon and nitrogen in the purine ring.
13. What are proto-oncogenes? How are they activated?
14. Mention the vectors used in Recombinant DNA technology and write their importance.
15. Write van den Bergh test and its interpretation in Hepatic Jaundice.
16. What are growth factors? Give two examples.
17. Write three detoxification reactions by conjugation mechanism.
18. Mention the advantages of automation in clinical biochemistry laboratory.
19. Write three reactions of purine salvage pathway.
20. What are Thalasemias? What are the defects in Alpha and Beta Thalasemias?
Page 1 of 3
QP CODE : 1025
21 i) Drug which inhibits xanthine oxidase is
A. Allopurinol
B. Aspirin
C. Colchicine
D. Probenicid
21 ii) Hypoalbuminemia is not seen in
A. Chronic liver disease
B. Nephrotic syndrome
C. Hemoconcentration
D. Protein energy malnutrition
21 iii) Which of the following is an inhibitor of RNA synthesis?

A. Rifampicin
B. Ciprofloxacin
C. Novobiocin
D. Adraiamycin
21 iv) Which of the following is an example for sulphur containing amino acid?
A. Phenylalanine
B. Glycine
C. Threonine
D. Cysteine
21 v) Which of the following is purely Ketogenic amino acid?

A. Proline
B. Glycine
C. Alanine
D. Leucine
22 i) In DNA number of hydrogen bonds between Guanine and Cytosine is

A. One
B. Two
C. Three
D. Four
22 ii) Tumor marker for colorectal cancer is

A. Carcinoembryonic antigen (CEA)
B. Alpha-fetoprotein
C. Calcitonin
D.  - HCG
22 iii) Nitrogen atoms of urea are derived from ammonia and

A. Aspartic acid
B. Alanine
C. Histidine
D. Valine
22 iv) Normal value of plasma osmolality is

A. 185 to 200 milliosm/kg
B. 285 to 300 milliosm/kg
C. 385 to 400 milliosm/kg
D. 485 to 500 milliosm/kg
22 v) Reproducibility of results is best described as:

A. Sensitivity
B. Specificity
C. Precision
Page 2 of 3
QP CODE : 1025
D. Accuracy
******
Page 3 of 3
MBBS Phase – I Degree Examination - 17-Jul-2023

Q.P. CODE: 1079

1. What are Lipoproteins? How are they classified? How is Chylomicrons metabolized?

2. Define Enzyme Inhibition. Discuss the Competitive Inhibition with examples.
3. What are Mucopolysaccharides? Write their biomedical significance.
4. Briefly explain how Acetyl CoA is completely oxidized via Kreb’s cycle.
5. Urea cycle.
6. Formation and utilization of ketone bodies.

7. Beri Beri.
8. Phenylketonuria
9. State three biochemical changes that occur during Starvation.
10. Detoxification by Conjugation.
11. Name the diagnostic enzymes for Myocardial Infarction and Liver dysfunction.
*****
First Phase MBBS Degree Examination – 17-Jul-2023

QP Code: 1080

1. What is the normal pH of blood? Discuss the role of kidneys in the maintenance of acid-base
balance.

2. Describe transcription process. Add a note on its regulation.
3. (BMR). Basal Metabolic Rate (BMR)
4. Dietary fibre.
5. Gout.
6. Metabolic acidosis.
7. Oncogenes
8. Clearance test.
9. Free radicals
10. (PCR) Polymerase Chain Reaction (PCR)
11. Lac operon
*****

Biochemistry Q P 2011 - 2023

Uploaded by

Document Information

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

Biochemistry Q P 2011 - 2023

Uploaded by

Copyright:

Available Formats

1079_2011_1_S263

Rajiv Gandhi University of Health Sciences

BIOCHEMISTRY (RS 2 & RS 3)

QP Code: 1079 – PAPER I (Max. Marks: 50)

LONG ESSAY 1 X 10 = 10 Marks

SHORT ESSAY 5 X 5 = 25 Marks

SHORT ANSWERS 5 X 3 = 15 Marks

QP Code: 1080 – PAPER II (Max. Marks: 50)

LONG ESSAY 1 X 10 = 10 Marks

SHORT ESSAY 5 X 5 = 25 Marks

SHORT ANSWERS 5 X 3 = 15 Marks

Rajiv Gandhi University of Health Sciences

BIOCHEMISTRY (RS 2 & RS 3)

LONG ESSAY 1 X 10 = 10 Marks

SHORT ESSAY 5 X 5 = 25 Marks

SHORT ANSWERS 5 X 3 = 15 r-.1arks

QP Code: 1080 - PAPER II (Max. Marks: 50)

SHORT ESSAY 5 X 5 = 25 Marks

SHORT ANSWERS 5 X 3 = 15 Marks

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

4. Classify lipoproteins and write the functions of each lipoprotein.

SHORT ANSWERS 5 x 3 = 15 Marks

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

5. What is a restriction endonuclease? Explain their role in recombinant DNA technology.

SHORT ANSWERS 5 x 3 = 15 Marks

Use separate answer books for section A and Section B

4. Clinical importance of enzymes in assessment of cardiac disease & liver function

Use separate answer books for section A and Section B

4. Describe with an example regulation of gene expression.

5. What do you mean by gene therapy? Discuss its application in medicine.

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

5. What is biotransformation? Discuss the different phases of biotransformation with an example.

Components of electron transport chain

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

5. Discuss the biochemical changes during starvation

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

SHORT ANSWERS 5 x 3 = 15 Marks

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

SHORT ANSWERS 5 x 3 = 15 Marks

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

4. Describe the conversion of methionine to cysteine. Add a note on homocystinuria.

5. Outline the synthesis of epinephrine and give its functions.

SHORT ANSWERS 5 x 3 = 15 Marks

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

4. Explain the role of kidneys in acid base regulation.

5. What is a balanced diet? Discuss the components of a balanced diet.

Use separate answer books for section A and Section B

LONG ESSAYS 1 x 10 = 10 Marks

SHORT ESSAYS 5 x 5 = 25 Marks

4. What are mucopolysaccharides. Give their importance with examples.