CELL BIOLOGY

Cell Organelle (SAQ/BAQ)

1. Enumerate the functions of mitochondria
2. What are marker enzymes?
3. What are the enzymes present in lysosomes? Mention their function.
4. What are microsomes?
5. Mention one function each of the Golgi apparatus and Ribosomes.
6. Name the marker enzyme for endoplasmic reticulum of cell.
7. Mention the metabolic functions of endoplasmic reticulum.
8. Name the marker enzymes for a) Mitochondria b) Lysosome c) Golgi apparatus d) Cytosol. List any
four metabolic pathways present in mitochondria.
Cell Membrane (SAQ/BAQ)
1. Describe the fluid mosaic model of the bio-membrane using suitable diagram.
2. Cytoskeleton
3. Write four structural features of cell membrane
4. Give the chemical composition of cell membrane
Transport Mechanisms (SAQ/BAQ)
1. What is sodium-potassium pump?
2. Explain the structure of a typical biological membrane with a labeled diagram.
3. What are the various transport mechanisms across cell membrane?
4. Explain active transport with suitable example and illustrations.

ETC & Oxidative Phosphorylation

1. Many reactions though thermodynamically unfavorable take place in an appreciable rate in our body.
Explain what modalities human systems utilize to overcome this thermodynamic barrier? (2)
2. What is meant by DG0 in thermodynamics of biochemical reactions? Explain how a biochemical
reaction can occur spontaneously even when DG0 is positive. How does an enzyme accelerate a
reaction? Do enzymes have any influence on DG0? (1+2+1+1 = 5)
3. What are high energy compounds? Give example.
4. How ATP concentration is maintained relatively constant during muscular contraction.
5. What is substrate level phosphorylation? Give two examples.
6. What is difference between SLP and OP?
7. Describe the organization of ETC. explain oxidative phosphorylation. How does cyanide influence the
process. CHEMIOSMOTIC THEORY
8. Coenzyme Q
9. Write a note on ATP synthase and mention mechanism of ATP biosynthesis.
10. What are inhibitors of ETC? How are they calssified?
11. Cyanide & 2,3 DNP
12. What are uncouplers of oxidative phosphorylation? Give an example.
13. Reversal of ETC.
14. State the rationale: FADH2 has a P:O ratio of 2.

Enzymes
Long questions
 1. Classify enzymes with suitable examples. Discuss the factors affecting enzyme activity.
2. What are salient features of active site of enzyme?
3. Explain different type of enzyme inhibition. How are they identified based on line-weaver burke
plot?
4. How does an enzyme accelerate a reaction? What is the significance of Km value? How
the
difference in Km value between gulcokinase and hexokinase does suit its functions?
5. What is the effect of substrate concentration on rate of enzyme catalyzed reaction? Add a

note on Km.

Short questions
1. Give two examples for zinc metallo proteins? (1)
2. Name two enzymes, which require PLP as coenzyme (1)
3. Name an enzyme that belongs to the group “Ligase” in modern classification. (1)
4. The proteolytic enzyme pepsin belongs to which class of enzymes? Does it require a coenzyme
for its action?
5. Explain the meaning of the terms. (a) Exopeptidases (b) Endopeptidases by giving examples
6. To which class of enzymes “Transketolase” belongs? Give one reaction catalyzed by it.
1. Which metal is required for the activity of Carbonic anhydrase? (1)
7. Which coenzyme participates in most carboxylation reactions?
8. Name two digestive enzymes that act in alkaline pH. (1)
9. Which enzyme is responsible for the dietary glycogen digestion? How does it act? (2)
10. Name the digestive enzyme, which hydrolyses milk sugar. (1)
11. Name the proteolytic enzymes present in gastric juice and pancreatic juice. Name the enzymes
that digest protein from the N- terminal end and the enzyme that digests the protein from the
C- terminal end. (2)
12. Name the classes of enzymes that do not require coenzymes. (1)
13.
14. What is Km value? What is its significance?
15. What are isoenzymes? Give two examples.
16. Describe the features of competitive inhibition. Give three examples with their clinical
importance.
17. Describe suicide inhibition
18. What are various clinically useful enzymes.
19. Illustrate the typical changes of serum CK, CK-MB, AST, LDH in MI and muscular
dystrophy.
20. Treatment of a patient with methanol poisoning is based on the principle of competitive
inhibition. Explain how.
21. How does allopurinol affect the kinetics of Xanthine oxidase? Explain with the help of a graph.
22. Give an example for an enzyme belonging to the class of oxido-reductases. Name the
substrate, coenzyme and product.
23. Give an example of covalent modification of enzyme regulation.
24. Write a note on allosteric enzymes
25. What are ligases? Give two examples of reaction catalysed by ligases.
26. What is Michaelis-Menten equation? Write its significance.
27. Define coenzymes. Mention two examples. Indicate their functions
28. What are isoenzymes of ALP. Mention their importance.
29. How are the following activated? a. Pepsinogen b. Trypsinogen
 30. What is the normal level of serum ALP? Mention two important pathological conditions
where it is raised?
31. In which type of enzyme inhibition is the ‘inhibitor’ regarded as substrate analog? What
is the inhibitor and substrate for xanthine oxidase?
32. Write the clinical significance of serum amylase
33. Briefly describe covalent modification in enzyme regulation taking glycogen
phosphorylase
34. Give the diagnostic significance of a) Gamma glutamyl transpeptidase b) Lactate
dehydrogenase
35. To which main class of enzymes do the following belong:
a. Pyruvate carboxylase b. Pyruvate decarboxylase
36. 5. What is the diagnostic significance of elevated AST in blood.
37. 6. Write the diagnostic significance of increased ALT in blood.
38. Why does high temperature decrease enzyme activity?
39. Write in detail about the enzyme markers in diseases of skeletal muscle, liver, pancreas
diseases, and
Prostate (5)

ACID BASE BALANCE

Long Questions
1. What is the normal pH of the blood? Explain the different mechanism involved in the
maintenance (regulation) of the acid base balance
Short Questions
1. How does kidneys help in maintain pH of blood?
2. Describe the role of extracellular and intracellular buffers in maintaining acid base balance?
3. What is metabolic acidosis? Enumerate its causes and biochemical changes (PCO 2, pH, HCOO3-).
What are compensatory mechanisms?
4. Explain the acid base disturbance that is seen in uncontrolled diabetes mellitus.
5. What is meant by Anion-gap? What is its importance?
6. Write Henderson-Hasselbalch equation. How parameters of this equation is altered in respiratory
acidosis?
7. What are the parameters used in assessment of acid base status of blood? Give their normal levels.
8. Indicate the nature of disturbance in acid base balance that may develop in hyperventilation.
9. Which amino acid plays an important role in kidney in maintaining pH homeostatis?

Hemoglobin Structure-Function & Hemoglobinopathies

Long questions
1. Explain the structural organization of Hemoglobin. Explain how the structure of hemoglobin is
carrying out its function?
Short questions
1. Write factors that shift oxygen dissociation curve to right with help of suitable graph.
2. What is the role of 2,3 Bisphosphoglycerate? What is its significance?
3. What is P50? Explain the role of HbF in fetal life.
4. Name 3 abnormal hemoglobin. Indicate change in each case.
5. Sickle cell anemia (genetic defect, clinical features, electrophoretic picture)
6. What is mechanism of carbon monoxide poisoning?
7. What is the molecular basis of α and β thalassemia? Enumerate various types of thalassemia.
8. Write a note on hydrops fetalis & β thalassemia major.
Heme Metabolism
Long questions
1. Describe the catabolism of heme to bilirubin in the body.
Short questions
1. How would you distinguish between various types of jaundice based on biochemical tests in plasma
and urine?
2. What is the principle of Van Den Berg test?
3. What is physiological jaundice? Which type of bilirubin is increased in it?

PORPHYRIAS
Long Questions
1. Discuss the pathway of heme synthesis.Write in detail about the biochemical basis,
symptoms,diagnosis and treatment of porphyries
Short Notes

1. Name the regulated step of Heme Synthesis.

2. Write in detail about classification of porphyria
3. What are Porphyrias? Write the biochemical defect in Acute Intermittent Porphyria
4. Write a short note on Acute Intermittent Porphyria.
5. What is the defect of Acute Intermittent Porphyria and porphyria cutanea tarda
6. Why certain drugs & other chemicals can precipitate an attack of Acute Intermittent
Porphyria.
7. What is zinc protoporphyrin? How is it useful diagnostically?
8. What is the most common type of porphyria? Describe its features.

Water soluble vitamins S

Long questions

1. Write the sources, requirements, deficiency manifestations, biochemical actions of Vit C.

2. Name three sulphur containing vitamins. Describe in detail the biochemical functions,
sources, daily requirement and deficiency manifestations of any one of them.Vitamin B1,
biotin, and pantothenic acid contain small amounts of sulfur.
3. Describe the chemistry, biochemical functions, sources, daily requirements and deficiency
manifestations of niacin.
4. Describe the biochemical roles of Ascorbic acid.
5. Write briefly on Thiamine with reference to its sources, daily requirements and biochemical
functions. Add a note on its deficiency symptoms.
6. Describe the sources, daily requirement, metabolic functions and deficiency
manifestations of pyridoxine
Short questions

1. Describe the biological roles of Ascorbic acid.

2. Write down five reactions requiring pyridoxine as coenzyme
3. Mention any three reactions in which niacin functions as a coenzyme. Describe the
deficiency manifestation of vitamin B12.
4. Cobalt forms an integral part of one of the important vitamins. Name
the vitamin. Describe the biochemical function.
5. What are the coenzyme forms of vit B12? Give a reaction where each is used.
6. Write the coenzymic role of thiamine pyrophosphate
7. Manifestation of pellagra
8. What are the metabolic roles of thiamine in body?
9. Why does the dietary requirement of pyridoxine increase with high protein diet?
10. Write a note on beriberi
11. List three types of biochemical reactions requiring biotin as co-enzyme
12. In scurvy there is a increased tendency for bleeding- explain with reasons
13. Write about FIGLU
14. Name the antagonist for folic acid and pyridoxine.
15. Write briefly on the absorption of vitamin B12.
16. Vitamin C plays a role in post translational modifications. Justify.
1. Which enzyme activity is estimated to detect riboflavin status?
2. Describe renal rickets.
3. What are anti-metabolites? Give one example.
17. Name three groups carried by folic acid.
18. What are the abnormal metabolites found in urine of patients with B12 deficiency? Explain
how folate is trapped in B12 deficiency and what is its consequence?
19. Why thiamine requirement does goes up in high carbohydrate diet?
20. What is Wernicke – Korsakoff syndrome?
21. Eskimos are reported to have a deficiency of thiamine due to their food habits. Why?
22. Give the coenzymic forms of Riboflavin. (2)
23. List out any two enzymes that utilize FMN as coenzyme. (2)
24. List out any four enzymes that utilize FAD+ as coenzyme. (2)
25. Give the relationship between tryptoaphan and Niacin. (2)
1. Give the coenzymic form of Pantothenic acid. (1)
2. Which vitamin deficiency leads to “Burning feet syndrome”? (1)
26. List out any two enzymes that utilize Pantothenic acid as coenzyme.
27. What are the dietary sources of Biotin? (1)
28. Which types of reactions are catalysed by Biotin? (1)
29. List out any two enzymes that utilize Biotin as coenzyme. (2)
30. Name a Biotin antagonist. How it prevents the action of Biotin? (2)
31. Intake of raw egg leads to biotin deficiency. Why?
32. Name an antagonist for pyridoxine. (1)
33. Explain why Dietary deficiency of Vitamin B 6 can lead to deficiency in pyridine nucleotide
synthesis? (2)
34. Why is pellagra like features likely to be seen in a patient with carcinoid syndrome? (2)
35. Explain why pyridoxine is administered to a patients undergoing antituberculosis therapy?
(2)
36. List out any four enzymes that utilize PLP as coenzyme. (2)
37. Name the Vitamin required for transamination reaction. (1)
38. What are the dietary sources of folic acid? (1)
39. Give the other name of folic acid. (1)
40. What are the coenzymic forms of folic acid? (2)
41. Outline the biochemical basis of histidine load test carried out for the assessment of folic
acid deficiency (2)
42. Para amino Benzoate is a growth factor for some microorganism and antagonistic to the
bacteriostatic action of sulfonamides. Explain the statement (2)
43. Name the one carbon compounds? What is the role of Folic acid and B 12 in their
metabolism? What is meant by Folate trap? (7)
44. List out the folate antagonist and mention how they act? (2)
45. A patient has been diagnosed as having megaloblastic anemia.
a. Which vitamin deficiencies can cause anemia? (2)

46. Why humans and guinea pigs are not able to synthesis vitamin C? (1)
47. “Vitamin-C plays a role in post translational modification”. Justify. (2)

MINERAL METABOLISM

Calcium

1. Hormones that regulate the serum calcium level.

2. What is the normal plasma calcium level? Name 2 hormones which elevate it ?
3. What are the forms of plasma Calcium?
4. Enumerate the factors that affect the absorption of Calcium?
5. What are the factors that maintain ionized Calcium in plasma? Discuss the role of each of them.
6. How is the calcium homeostasis affected in kidney diseases?
7. What are the functions of calcium? Discuss the factors that influence the absorption of calcium?
How is plasma calcium maintained? What are the changes in plasma calcium, phosphorus and
alkaline phosphatase levels in Rickets and Hyperparathyroidism?
8. What is the role of Parathormone on the synthesis of Calcitriol?
9. Why is dietary calcium not absorbed in a patient with renal damage?
10. When a person develops hypocalcemia, how does his body try to bring it back to normal level?
Iron

1. Absorption of Iron
2. Transport of Iron
3. Hemosiderosis
4. What are the transport and storage forms of Iron?
5. What is the average iron absorption in a woman in reproductive age group?
6. What is the RDA of iron? How much of it is absorbed? Describe the factor affecting the absorption of
iron?
7. What is the function of transferrin?
8. What is haemochromatosis ? What is bronze diabetes?
9. Define mucosal block theory in iron absorption and name two factors increasing iron absorption
10. Name the dietary factors promoting Iron absorption?

Copper

1. Discuss the role of dietary copper in the body.

2. Can copper deficiency cause anemia? How?
3. Write briefly on Wilson’s disease.
4. Name three enzymes that require copper as cofactor.
Zinc

1. Metabolic role of Zinc.

2. Manifestation of zinc deficiency in the human body
Selenium, Cobalt, Iodine & other trace elements

1. Give one function for each of the following:

a) Selenium
b) Cobalt
c) Iodine
2. Name 4 trace elements and mention one function for each.
3. Mention the selenium requiring enzymes in the body
4. Tocopherol has sparing effect on requirement of selenium. Explain?
5. Enumerate two enzymes that require Magnesium as cofactor
6. Name a Zinc containing protein in saliva. Mention its function
7. Of which mineral is Milk a rich source?
8. Define Goitrogens. Give two examples
9. Classify minerals with examples.
10. Name four biologically important compounds where minerals are integral components
11. What are the consequences of giving high doses of magnesium to a normal person
12. Name the metalloenzyme of each of the following element.
a. Molybdenum b) Manganese c) Selenium d) Cobalt
13. Acrodermatitis enteropathica
14. Selenium