Question Bank of Frequently Asked Questions

Biochemistry, Ist MBBS , 19-06-2013

1. Carbohydrate Chemistry
1. Classify carbohydrates with examples; write biological importance of any two. (3/4)
2. Give 2 examples for each of the following. (3)
a) Aldopentoses b) Ketoses c) Mucopolysaccharides
3. Polysaccharides. (3/4)
4. Difference between Starch and Glycogen. (3)
5. Glycosaminoglycans (3)
6. What are mucopolysaccharides? Name the functions and composition of any four
mucopolysaccharides. (4)
7. Name Mucopolysaccharides. Mention their function (3)
2. Protein Chemistry
1. What are essential amino acids? Name them. (3)
2. Essential amino acids (3)
3. Name three biologically active peptides. Mention their functions. (3)
4. Classify proteins based on function. Give one example for each class (4)
5. Classify proteins based on composition giving suitable examples. (3)
6. What is primary structure of proteins? Explain its importance (3)
7. Explain the biochemical basis: a) Primary structure of a protein decides its function.
(3)
8. Write short note on Secondary structure of protein. (3)
9. Bonds that contribute to the protein structure. (3)
10. What is quaternary structure of protein? Give examples for proteins having quaternary
structure. (3)
11. Denaturation. (3)
12. What is meant by denaturation of proteins? Name four denaturing agents. (3)
13. Explain the biochemical basis: Proteins lose their biological activity when denatured. (3)
14. Give 2 examples for each of the following. (1 mark each)
a) Peptides b) Fibrous proteins c)Transport proteins d) Secondary protein structures
3. Lipid Chemistry
1. Classify lipids with examples (3/4)
2. Essential fatty acids (3)
3. Name the essential fatty acids and one function of EFA (3)
4. Name essential fatty acids and mention their functions (3)
5. What are eicosanoids? Mention them with their functions. (3)
6. Compound lipids (3)
7. What are phospholipids? Give 3 examples. Mention their functions (3)
8. Write short notes on a) Lecithin b) PUFA (3)
9. Give examples and compositions of a) Glycophospholipid b) Sphingophospholipid (3 )
10. Give 3 examples for each of the following. a) Amphipathic lipids b) Glycolipids (3)
11. What are lipoproteins? Describe their composition and functions. Explain lipoprotein
structure with a diagram (3/4)
4. Nucleic acid Chemistry
1. Name 3 biologically important nucleotides. Mention their functions. (3)
2. Write on Watson - Crick Model of DNA structure. (4)
3. Write briefly on secondary structure of DNA. (3/4)
4. Mention the functions of DNA. (3)
5. Compare and contrast DNA and RNA in terms of their chemical composition, structure
and function. (3)
6. Differences between DNA and RNA (3)
7. Types of RNA and their function (3/4)
8. Structure and functions of transfer RNA. (3/4)
5. Enzymes
1. What are enzymes? Classify them giving one example each. Indicate the reaction
catalyzed by the enzyme in each class. (5)
2. Classify enzymes with suitable examples. (3)
3. Give 2 examples for each of the following. (1 mark each)
a) Oxidoreductases b) Transferases c) Hydrolases d) Lyases e) Isomerases f) Ligases
4. Km value. (3)
5. Define Km value. What is its significance? (3)
6. What are enzymes? Describe the factors affecting velocity of enzyme-catalyzed reaction.
(5)
7. Give the features of competitive inhibition of enzyme. Explain its importance in the
clinical medicine with an appropriate example. (3/4)
8. Define competitive inhibition. Give two examples of competitive inhibitors used
therapeutically. (3/4)
9. Zymogens. (3)
10. Proenzymes (3/4)
11. What are proenzymes? Give two examples. (3)
12. Give an example of allosteric enzyme and name modulators for the enzyme. (3)
13. What are isoenzymes? Name the isoenzymes forms of LDH and CK. What are their
clinical significance? (4)
14. Name five enzymes of diagnostic significance. Give the normal serum levels and one
clinical condition associated with their increase. (4)
15. Explain enzyme profile in Myocardial infarction. (3)
16. Therapeutic uses of enzymes. (3)
6. Membranes and Sub-cellular Structures
1. Write a note on Fluid Mosaic model of the cell membrane. (3)
2. Active transport (3)
3. Explain active transport with an example. (3)
4. Mitochondrial structure and important functions (3)
1. Digestion & Absorption:
1. Digestion of carbohydrates in diet. (3/4)
2. Describe digestion of starch to glucose. (3/4)
3. Describe with the help of a diagram how glucose is absorbed in the intestine. (3)
4. Describe the absorption of glucose (3)
5. Glucose absorption (3/4)
6. Lactose intolerance (3/4)
7. What are zymogens? Give two examples. (3)
8. Zymogens. (3)
2. Carbohydrate Metabolism
1. Enumerate the glycolytic pathway with energetics . (5)
2. Describe the reactions of glycolysis. Add a note on the net ATP yield under aerobic and
anaerobic conditions. (5)
3. Number of ATP molecules formed in glucose oxidation. (3)

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4. Describe Rapaport – Leubering cycle. What is its significance? (3/4)
5. What is substrate level phosphorylation? Give two examples. (3)
6. Mention the different sources of acetyl CoA. (3)
7. Describe the oxidation of acetyl CoA in the citric acid (TCA) cycle. Discuss the
energetics of the TCA cycle. (5)
8. What is anaplerosis? What is its significance? (3)
9. Describe the reactions of pentose phosphate pathway. Mention the significance of this
pathway. (5)
10. Describe the HMP shunt pathway and state its significance. (5)
11. Metabolic significance of HMP shunt pathway. (3/4)
12. Glycogenesis (3/4)
13. Describe glycogenolysis. Add a note on the glycogen storage diseases. (5)
14. What is Glycogen? Describe the process of Glycogenolysis. (5)
15. Glycogen storage diseases. (3/4)
16. Von Gierke’s disease. (3)
17. Indicate the biochemical defect in a) Von Gierke’s disease b) Fructose intolerance
c) galactosemia. (3)
18. Describe the reactions of gluconeogenesis. Mention its significance. (5)
19. Define Gluconeogenesis. How is lactate converted to glucose in the body? (5)
20. Give 3 examples for each of the following. (3)
a) Glycogen storage diseases b) Key enzymes of gluconeogenesis.
21. Write short notes on a) Cori Cycle b) Essential fructosuria. (3)
22. Galactosemia. (3/4)
3. Lipid Metabolism
1. Describe the various reactions involved in beta-oxidation of fatty acids. Add a note on its
energetics. (5)
2. Mention the different sources of acetyl CoA. (3)
3. Name the ketone bodies. Mention two conditions causing ketosis. (3)
9. Name the biochemical defect in a) Niemann-Pick disease and b) Gaucher’s disease.
(3/4)
10. Name four substances synthesized from cholesterol? (2)
11. List the derivatives of cholesterol. Describe the biomedical importance of three
derivatives of cholesterol. (3/4)
12. What are the biologically important compounds derived from cholesterol?
(3/4)
13. What is normal serum level of cholesterol? Name its four biological functions? (3)
14. Classify lipoproteins. Mention their function. (3/4)
15. Mention the causes of fatty liver. (3)
16. What is Fatty liver? Explain its causes. (3/4)
17. Fatty liver and lipotropic factors (3/4)

5. Oxidative Phosphorylation
1. Write the components of electron transport chain. Indicate the sites of ATP formation
during electron transport. Name two inhibitors of electron transport. (3/4)
2. Components of electron transport chain and sites of A.T.P formation. (3)
3. Mechanism of oxidative phosphorylation (3/4)
4. What is oxidative phosphorylation? Explain its mechanism. Mention its inhibitors.(4)
6. Glucose homeostasis, starvation, diabetes mellitus
1. What is the normal blood glucose level? Describe the regulation of blood glucose. (5)
2. Describe the hormonal regulation of blood sugar level. (5)

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3. Explain the role of insulin in glucose homeostasis. (3/4)
4. Oral Glucose tolerance test (3/4)
5. Detection of reducing sugar in urine. (3)
7. Protein & Amino acid Metabolism
1. Explain the transamination reaction. (3/4 )
2. What are the sources of ammonia in the body? Describe how ammonia is detoxified in the
body and name two inborn errors associated with this process. (5)
3. Urea formation in liver (3/4)
4. Describe the urea cycle. What is the normal blood urea level? Name two conditions in
which blood urea level increases. (5)
5. Enumerate the compounds formed from glycine, giving their biochemical importance.
Why glycine is nutritionally non-essential? (5)
6. Metabolic role of glycine (3/4)
7. Name any five products formed from glycine (3/4)
8. S-Adenosyl Methionine (3)
9. Mention the enzyme defect in phenylketonuria and homocystinuria (3)
10. Give 3 examples for each of the following. (3)
a) Important compounds derived from tyrosine b) Inherited disorders of tyrosine
metabolism
11. Name the biochemical defect in Phenylketonuria (3)
12. PKU (3)
13. Alkaptonuria. (3)
14. Name two products synthesized from Tryptophan. (3)
15. Name the enzyme defect maple syrup urine disease. (3)
16. Name the biochemical defect in Maple syrup urine disease. (3)
17. Name the biochemical defect in the following disorders of amino acid metabolism.
a) Phenylketonuria b) Alkaptonuria c) Maple syrup urine disease d) Albinism
e) Homocystinuria. f) Hartnup’s disease (3)
14. Heme Metabolism
1. Name five heme proteins and their functions. (3/4)
2. Give an account of Heme biosynthesis. Write briefly on hepatic porphyrias. (5)
3. What are porphyrias? How are they classified? Name the enzymatic defect and
biochemical findings in any one of the porphyrias. (3/4)
4. What are porphyrias? Name one disorder indicating the underlying cause. (3)
5. Acute intermittent porphyria. (3)
6. Formation and fate of bilirubin in the body (3/4)
7. How bilirubin is formed and detoxified in the body. (3/4)
8. Unconjugated hyperbilirubinemia (3/4)
9. What is the normal level of bilirubin in serum? Define Jaundice. Mention one cause for
Different types of Jaundice (3)
10. Hemolytic Jaundice. (3/4)
11. Laboratory diagnosis of hemolytic jaundice. (3)
12. Biochemical changes in obstructive jaundice. (3/4)
13. Van den Bergh reaction. (3)
14. Explain the biochemical basis: a) urobilinogen is absent in urine in obstructive jaundice.
b) In obstructive jaundice feces is clay colored. c) ALT and AST levels are raised in the
serum of hepatic jaundice.
15. Hemoglobin –Structure, Function, Abnormal Hb
1. Methemoglobin (3/4)

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2. Discuss the manifestation molecular basis and laboratory diagnosis of Sickle cell disease.
What is the biological advantage of Sickle cell trait? (3/4)
3. Sickle cell hemoglobin (3/4)
16. Plasma Proteins
1. What is the normal level of plasma proteins? Name a disease which features
hypoalbuminemia. (3)
2. Enumerate the functions of albumin. Mention the cause of hypoalbuminemia and
consequences of hypoalbuminemia. (4)
3. Name the immunoglobulins. Describe their functions. (4)
4. Transport proteins of blood (3)
17. Detoxification
1. Different mechanisms of detoxification with one example each (4)
2. Conjugation as detoxification mechanism (3)
18. Function Tests
1. Describe liver function test and their significance. (4)
2. Serum enzymes estimated to access the liver function (3)
3. Laboratory diagnosis of hemolytic jaundice. (3)
4. Name clearance tests used to asses kidney function. Explain any one of the clearance
tests and mention its significance. Mention the normal levels of serum urea and
creatinine (4)
5. Creatinine clearance test. (3)
19. Acid-Base Balance
1. What is pH? Add a note on the biological significance of pH. (3)
2. Importance of Henderson-Hesselbach equation (3)
3. Define pH and buffer. Mention the buffer systems present in plasma, erythrocytes and
urine. (3)
4. Define buffers. Name the blood buffer systems (3)
5. What is the normal pH of blood? Name the mechanisms to maintain it. (3)
6. Bicarbonate buffer system of blood (3)
7. Define pH. What is the reference range of pH of blood? Explain the role of bicarbonate
buffer in the maintenance of acid-base balance of the body. (3)
8. Explain the biochemical basis: Bicarbonate buffer is the most important blood buffer. (3)
9. Renal regulation and respiratory regulation of body pH. (3)
10. Metabolic Acidosis (3)
11. Explain the biochemical basis: a) Acidosis in ketosis b) Increase in depth and rate of
breathing is observed in metabolic acidosis. (3)
12. Mention two causes and features of metabolic acidosis (3)
13. Write the salient features of metabolic alkalosis. (3)
14. What is anion gap? Mention two causes for increased anion gap? (3)
15. Define respiratory acidosis? Mention the causes and biochemical findings in respiratory
acidosis. (3)
20. Vitamins
1. Describe the chemistry, sources, functions and deficiency manifestations of vitamin A.
(5)
2. Enumerate the functions and deficiency manifestations of vitamin A. (3)
3. Visual cycle (3)
4. Describe the chemistry, sources, functions and deficiency manifestations of vitamin D.
(5)
5. Describe the causes and features of Vitamin D deficiency. (3)

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6. Provitamins (3)
7. Sources and function of Vit. K (3)
8. Explain the following aspects of thiamin. (3)
a) Coenzyme form b) Biochemical functions and c) Deficiency
9. Coenzyme role of thiamine and Riboflavin. (3)
10. Explain the following aspects of riboflavin.
a) Coenzyme form b) Biochemical functions and c) Deficiency (3)
11. Deficiency manifestation of Niacin. (3)
12. Pellagra. (3)
13. Biochemical functions of pyridoxine. (3)
14. Chemistry, sources and daily requirements of folic acid (3)
15. Functions of folic acid. (3)
16. Name the biochemical function of vitamin B12. (3)
17. Discuss the chemistry, source, requirement, metabolic functions and deficiency
manifestations of ascorbic acid in the human body. (5)
18. What are Antioxidants. Name chain breaking and preventive antioxidants. (3)
21. Minerals
1. Write in detail about the distribution of calcium in the body, its functions and regulation
of serum levels. (5)
2. Mention the sources, daily requirements, functions and deficiency symptoms of calcium.
Explain how serum level of calcium is regulated. (5)
3. What is the normal serum calcium level? Explain its regulation. (3)
4. Sources, daily requirements and physiological role of iron (3)
5. Describe the absorption and transport of iron. (3)
6. Describe the functions and absorption of iron. (3)
7. Biochemical functions of Copper. (3)
8. Ceruloplasmin. (3)
9. Functions of zinc and selenium. (3)
10. Describe the functions of iodine and fluorine (3)
11. Fluorosis (3)
12. Name the serum electrolytes and give their normal values. (3)
22. Purine & Pyrimidine Metabolism
1. Mention the Origin of Carbon and Nitrogen Atom in Purine Ring. (3)
2. Sources of various atoms of purine ring. (3)
3. Describe two reactions of salvage pathway of purine nucleotide synthesis. (3)
4. Catabolism of purines (3)
5. Gout. (3)
6. What is gout? Mention two causes of gout. (3)
7. Describe the causes and features of hyperuremia. Mention the drugs to lower plasma uric
acid level. (4)
23. Genetics
1. What is Replication? Describe the steps of replication. (3)
2. What is transcription? Describe the steps of transcription. (5)
3. Name the posttranscriptional modification of mRNA (3)
4. Salient features of genetic code (3)
5. What is mutation? Give an account on point mutation. (3)
6. Explain the steps of activation, initiation, elongation & termination of protein
biosynthesis. (5)
7. What are restriction Endonucleases? Give two examples. (3)
8. Discuss in detail recombinant DNA technology and its clinical application. (5)

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9. What is Polymerase Chain Reaction (PCR)? Mention application of PCR. (3)
10. Gene therapy (3)
24. Nutrition
1.Define respiratory quotient. Write the RQ values of carbohydrates, lipids and proteins.(3)
2.Define calorific value. Mention the calorific value of carbohydrate, protein and fat. (3)
3.Define BMR. What is the normal BMR value of adult man? Enumerate six factors affecting
BMR. (4)
4.BMR (Basal Metabolic Rate). (3)
5.Balanced diet (4)
6.What are dietary fibers? Write two examples. Enumerate the role of dietary fiber. (3)
7. Describe the causes and features of Kwashiorkar and Marasmus. (3)
8.List two differences between marasmus and kwashiorkor. (3)
9.Protein calorie malnutrition (3)
25. Radioisotopes
1. Mention two isotopes and mention their application in medicine (3)
26. Techniques
1.ELISA (3)
27. Hormones
1.Classify Hormones with examples. (3)
2.General mechanism of action of steroid hormones (3)
3.Mechanisms of action of insulin (3)
28. Cancer
1.Name three important growth factors and mention their function (3)
2.What are oncogenes? Give two examples. (3)
3.Mention four tumor markers with their significance (3)
31. Free Radicals/Antioxidants
1.Define Free Radicals. How free radicals are generated in the body? (3)
32. Clinical Biochemistry
1. Give the normal blood level of the following
i. Fasting blood glucose
ii. Total protein
iii. Urea
iv. Bicarbonate
v. Sodium
vi. Potassium