VISION 100

BIOCHEMISTRY-CHAPTER WISE PREVIOUS

QUESTIONS

PAPER 1
1.CELL
 Structure of bio membrane
 Nucleosomes
 Ionophores
 Glucose transporters
2.CARBOHYDRATE
S
Essay questions

1. Describe by a flow diagram the reactions of glycolysis giving names of enzymes

involved. Explain its regulation and add a note on the energetic in aerobic &
anaerobic conditions. (6+2+2=10)
2. Enumerate irreversible steps of glycolysis with the enzymes involved/ Mention
any two key enzymes of glycolysis
3. Explain in detail glycogenesis and glycogenolysis. Mention the enzyme defects in
any two of glycogen storage disorders (4+4+2=10)
4. Define HMP shunt pathway and mention its significance/Significance of HMP
shunt pathway/ Importance of HMP shunt pathway
5. Trace the pathway of gluconeogenesis starting from alanine/ Glucose
Alanine cycle. Mention its significance. Mention the key enzymes and how
they are regulated. (5+3+2=10)
Shortnotes

1. Define gluconeogenesis. Name the gluconeogenic substrates

2. Kreb’s cycle
3. Name two carbon dioxide releasing steps in the TCA cycle/ Why TCA cycle is called
amphibolic
4. Describe glycogen metabolism
5. Complication of Diabetes mellitus
6. Diagnosis and monitoring of diabetes mellitus
7. Structure of human insulin/ Discuss the primary structure of human insulin
8. Glycation of haemoglobin and it's significances
9. Gluconeogenesis/ Discuss the significance of gluconeogenesis
10. Key enzymes of gluconeogenesis
11. Deficient enzyme and clinical features in galactosemia
12. Enzyme defect in lactose intolerance
13. Glucose transporters
14. Glycosaminoglycans/ What are glycosamino glycans. List two
examples with its functions?
15. Mention two glycogen storage diseases with their deficient enzyme
16. Name the enzyme deficient in Von Gierke's disease
17. What is Gaucher’s disease? Mention two clinical featuresMention
the enzyme deficient in Tay Sach’s disease
18. Cori’s cycle/Enzyme deficiency in Cori’s disease
19. Enzyme deficiency in Mc Ardle syndrome
20. Linkage present in sucrose
21.Classification of glycolipids
22. MutarotationWhat are epimers?/Epimer of glucose
23. Important product of Rapaport Lubering cycle in RBC/ List the functions of
Rapaport Lubering cycle
24. Fate of pyruvate
25. Lactose intolerance
26. Mention the reaction catalyzed by ATP-citrate lyase
27.Invert sugar
28. Essential pentosuria
29. Substrate level phosphorylation
30. Mention the biochemical defect in fructosuria
31. What is HbA1C and mention its clinical importance
32. Why sample for glucose estimation is collected in a fluoride bottle
33. Why starch can be utilized by humans but not cellulose
34. Two co-enzyme roles of NADPH
35. Normal blood level of urea and glucose
36. Benedict’s test
3.PROTIEN & AMINO
ACID
Essay
1. Name the sulphur containing amino acid. Discuss metabolism of the essential
amino acid of this group and add a note on associated inborn errors. (1+5+4=10
marks)
2. Important compounds derived from glycine/Mention the reactions by which
glycine is synthesized and catabolized. Add a note on the specialized products
formed and mention the disorders associated with glycine metabolism
(2+6+2=10)
3. Describe the various mechanisms by which ammonia is detoxified in the body&
add a note on urea cycle disorders(7+3=10)
4. Describe the pathway for synthesis of urea. Add a note on the regulation of the
pathway. Name two conditions in which blood urea is increased giving the
biochemical basis or enzyme defect (5+3+2=10)
Shortnotes

1. Define urea cycle and describe the reactions of urea cycle

2. Describe the reactions of urea cycle. Discuss the interrelationship between
urea cycle and citric acid cycle
3. Mention the normal blood urea level. Explain how urea is synthesized in the
body
4. Energy expenditure in Urea cycle
5. What is active methionine. Mention two examples of transmethylation
reaction.
6. Functional classification of proteins
7. Enumerate essential amino acids/ Name four essential amino acids.
8. Discuss the metabolism of phenyl alanine
9. Oroticaciduria
10. Homocystinurias
11. Phenylketonuria
12. Alkaptonurea/ Enzyme defect in alkaptonuria
13. Hartnup’s disease
14. Albinism
15. Ketogenic amino acids
16. Active methionine
17.Name two plasma transport proteins and mention their role
18. Polyamines/ Name the polyamines and mention its functions
19. Define transamination and explain by giving two examples. (1+4=5)
20. Trans methylation reactions/Mention three examples of trans
methylation reactions
21.VMA
22. Mention the chemical name of lecithin
23. Secondary structure of proteins
24. Define iso-electric pH, State properties of a protein at its isoelectric
pH
25. Name two transport proteins
26.Importance of glutamine
27. Glutathione/Biological action of glutathione
28. GABA
29. Covalent modification
30. Enzyme defect in maple syrup urine disease
31.Name the biochemical test for phenyl ketonuria
32.Normal level of serum albumin
33.Mention two examples of biologically important peptides
34.Mention two biologically active peptides
35.Denaturation/ Bond not broken in denaturation of protein
36.Heat coagulation
37.Sources of ammonia
38.Folate trap
39.Alpha helix
40.List the compounds formed from arginine
41.List two examples of mucopolysaccharides.
4.LIPIDS
Essay

1. Fatty acid synthase enzyme complex/ Name the rate-limiting enzyme in fatty
acid synthesis
2. Beta oxidation of fatty acids/ Define β-oxidation. Explain the reactions of β-
oxidation of palmitic acid. Add a note on its energetics. (2+5+3=10)
3. Explain the oxidation of palmitate in mitochondria. Describe how the process is
regulated. Mention the number of high energy phosphate bonds generate in
palmitate oxidation
4. Classify lipoproteins and mention the function of each.
5. Describe the role of lipoproteins in cholesterol transport.
 Shortnotes

1. What is the Normal serum cholesterol? Why HDL & LDL cholesterol are known
as good and bad cholesterol respectively ?
2. Functions of cholesterol
3. Regulation of cholesterol synthesis
4. Mention any two compounds derived from cholesterol
5. Essential fatty acids/ What are essential fatty acids? Enumerate them. List two
functions and one deficiency manifestation
6. Fatty liver/ What is the biochemical basis of fatty liver in alcoholism?
7. Name the ketone bodies. Describe the process of ketogenesis. List the
conditions that lead to ketoacidosis
8. LDL receptor
9. Give the normal serum values of HDL
10. Define carnitine and explain its role in oxidation of fatty acids
11.Carnitine shuttle/ Role of carnitine / Importance of Carnitine in lipid
metabolism
12.Name different lipases involved in lipid metabolism and mention its
functions
13.What is the role of bile salts in fat digestion and absorption.
14.Mention any four fate of acetyl CoAMention any two functions of
phospholipids
15.Plasma lipid profile
16.PUFA
17.Phosphatidic acid
18.Rate limiting reaction of cholesterol biosynthesisName the bile salts
and mention its functional significance
19.Ketosis
20.Classification of glycolipids
21.Four functions of phospholipids
22.Name the lung surfactant and mention its components/What is
23.Name the deficient enzyme in Niemann Pick disease
24.Plasma lipoprotein which is inversely correlated with coronary heart
disease
25.What are lipotropic factors. Enumerate three lipotropic factors/
Name four lipotropic factors
26.Why alcohol ingestion causes fatty liver
5.ENZYMES
Essays

1. Define enzymes. Classify enzymes according to IUB system with one example
each. Mention three enzymes commonly estimated after myocardial infarction
(1+3+6=10)
2. Define and classify enzymes. Give one example for each class and mention the
reaction catalysed.
3. What are enzymes. Explain briefly the factors affecting the velocity of enzyme
catalyzed reactions.
4. Explain different types of enzyme inhibition giving suitable examples
5. What is meant by suicide enzyme inhibition? Explain with one example
Shortnotes

1. List two clinical examples of competitive inhibition

2. Regulation of enzyme activity
3. Diagnostic significance of serum enzymes
4. Name different types of specificity shown by enzymes with examples/
Enumerate three types of enzyme specificity
5. Isoenzymes
6. Pro-enzymes
7. Allosteric enzymes
8. Ribozymes
9. Zymogen activation
10. What is the basis of curdling of milk?
11.Mention any two enzymes used as therapeutic agents
12.Define Km value/ Define Km value and state its importance
13.Enzymes as markers of myocardial infarction
14.Give the normal serum values of CPK-MB
15.Name the coenzyme required for transamination reactions
16.Name two therapeutic enzymes/Mention one therapeutic use of
enzymeMention the zinc containing enzymes
17.List two reactions where the folic acid is the co-enzyme
18.Michaelis Menten constantSignificance of km values
19.What are cathepsins
ETC and
TCA
1. Enumerate the components of electron transport chain. Describe the synthesis of
ATP. Indicate the site specific inhibitors. Mention two examples for uncouplers
(4+2+2+2=10)
2. TCA cycle and its various roles (6+2+2)
3. Diagrammatic representation of mitochondrial electron transport chain and location
of ATP synthesis (3+2=5)
4. Components and sequence of reactions occur in Electron transport chain
5. What is substrate level phosphorylation and mention two examples
6. Chemiosmotic mechanism of ATP synthesis.
7. Co-enzyme Q
8. Uncouplers of oxidative phosphorylation
9. Physiologic uncouplers