Ntruhs Biochemistry

BIOCHEMISTRY NTRUHS PREVIOUS QUESTION PAPERS
QUESTION PAPERS-M.B.B.S
BIO-CHEMISTRY FIRST YEAR-APRIL .2004 NEW REGULATIONS -500-A

MAX.MARKS:50 PAPER-1 TIME:2.30 HOURS
ANSWER ALL QUESTIONS
1.Explain the chemistry,daily allowance,sources,metabolic role and deficiency diseases

associated with vitamin C
(2+1+2+3+2=10)
2.Explain the types of Glycolysis in the body.Outline the steps of Glycolysis in Red blood
cells (erythrocytes).work-out the energetics of the pathway.(2+6+2=10)
Write short notes on: (5X4=20)
3.Prostaglandlns and their functions.
4.Inhibaitors and electron transport chain.
5.Factors influencing enzyme activity.
6.Thalassaemla.
7.Kwashlorkor.
8.Essential fatty acids(efa) (5X2=10)

9.Cori Cycle.
10.Anti Vitamins.
11.Defiency of Glucose-6-phosphate dehydrogenase.
12.Mentionthe normal serum values of the following blochemical parameters and their
clinical significances
A)SGOT
b)Serum acid phosphatase
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BIO-CHEMISTRY FIRST YEAR-APRIL .2004 NEW REGULATIONS 500-b

1.Explan the structural organization of a protein molecule and add a note on functions of
proteins in the body. (2+2+2+2+2=10)
2.what are nucleotides. Explain the sources of carbon and nitrogen atoms of purine and
pyrimidine rings. Explain the metabolic disorders associated with purine
metabolism.(2+4+4=10)
Write short notes on: (5X4=20)
3.i RN and its functions.

4.Explain detoxification with conjugation as an example.
5.Renal functions tests.
6.immunoglobulins.
7.biological role of fluorine in the body.
Write briefly on: (5x2=10)
8.Superoxide Dismutase.
9.Exons.
10.lsoelectric PH.
11.Biochemical findings in blood and urine in obstructine jaundice.
12.Absorption of iron.
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BIO-CHEMISTRY FIRST YEAR-OCT .2004 NEW REGULATIONS 500-A

1.Define Gluconeogenesis explain the pathway in humans from its predominant

precursor.Mention the key enzymes,their regulatory steps and signaificance of the
pathway. (1+4+2+2+1=10)
2.write the steps of biosynthesis of heme indicating the regulatory step.Add a note on
porphyrias.(6+1+3=10)
3.structural composition and functions of lipoproteins.
4.enzyme inhibitors and their clinical uses.
5.deficiency manifestations of pyridoxine.
6.Boyers binding change mechanism of ATP synthesis.
7.mechanisms of absorption of sugars from the gut.
8.a) BMR and its normol values (5x2=10)
b) Net protein utilization
9.The enzymes defective in
a)Refsums disease
b)Crigler-Najjar syndrome
10.cardiolipin and its clinical significance.
11."High energy" compound with four examples.
12.Biotransformation with 2 examples.

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BIO-CHEMISTRY FIRST YEAR-OCT .2004 NEW REGULATIONS 500-B
1.Define Ph and buffer. What is the normal range of blood PH ? Mention the Plasma and
RBC buffers Explain the different mechanisms of reglation of blood pH Add not on
metabolic acidosis. [1+1+2+4+2=10] 2.Name of the aromatic aminoacids. Describe the
metabolism of any one of them. Add a note on inbomerrors of metabolism of aminpacid
Mention laboratory test to detect it. (1+6+2+1=10)
3.Re plic ation of DNA
4.Deficiency disorders of iodinc
5.the plasma proteins mentioning their normal ranges and functions
6. Purinc salvage pathways
7.Renal function tests
8The enzyme and coenzyme required in the conversion of: (5x2=10)
a)Glycine to serinc . b )3-HYdroxy kynurenine to 3- b Hydroxy anthanilate
9. Biochemical defects in:
a)Cystiosis b)Hartnups disease
10.Degeneracy of genetics ode and name the aminoacids coded for by a single c
Adon
11.The post-transcriptional modification of RNAs.
12.Mechanisms of actions of insulin.

------------------------------------------------------------------------------------------------------QUESTION P
APERS-M.B.B.S
BIO-CHEMISTRY FIRST YEAR-MARCH/APRIL .2005 NEW REGULATIONS 500-A
1.Write the sources of daily allowance, chemistry functions and deficiency diseases with
relation of folic acid. (2+2+1+3+2=10)
2.Name the types of glycosuria.Describe the procedure of G.T.T. and its interpretation.
(4+4+2=10)
write short notes on: (5x4=20)
3.clinical significance of isoenzymes.
4.Fatty Liver.
5.Acute intermittent porphyria.
6.Specific Dynamic ac tion of food.

7.Oxidative phosphorylation
Write briefly: 5X2=10
8. Zymogems
9.Wilsons disease
10.Alpha fetoprotein
11.Name four esssntial amino acids
12.Mention the normal plasma values of the fallowing electrolytes:
a)Serum Sodium b)Serum potassium
c)Serum Calcium d)Serum Chloride

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BIO-CHEMISTRY FIRST YEAR-APRIL .2005 NEW REGULATIONS 500-B
ANSWER ALL QUESTIONS.
1.Explain the process of translation Under the following headings :a) activation
ofaminoacid b)Initiation c) elongation d) termination e) Post-translational processing.
(2+2+2+2+2=10)
2.Name body buffers.Explain how acid base balance is maintained in the body.Give the
normal leavels of Sodiem. Potassium,Chloride, Bicarbonate in the blood. (1+7+2=10)
WRITE Short notes on: (5X4=20)
3. Secondary structure ofproteins
4. Fluid Mosaic model
5. Serum calcium homeostasis
6 .DNA repair mechanisms
7.Glucocorticoids
8 Name clearance tests used to assess kidney function.Mention the significance of any one
clearance test. (5X2=10)
9.Anticancer agents
10. Compare and contrast DNA withRNA
11. Genetic code
12.Mention the biochemical defect in
a)Hemocystinuria b)parkinsonism
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BIO-CHEMISTRY FIRST YEAR-SEPT/OCT .2005 NEW REGULATIONS 500-A

ANSWER ALL QUESTIONS.1.How bilirubin is formed is formed in the body,How is it

detoxified? Explain its usefulness in the differential diagnosis of jaundice.Name the
abnormalities associated with bilirubin metabolism. (3+3+3+1=10)
2.Define gluconeogenesis.Name substrates for gluconeogenesis except lactate. Explain

gluconeogenesis starting from lactate.What is its importance. (1+2+5+2=10)
Write short notes on: (5x4=20)
3.Ketosis
4.Mucopolysaccharides
5.Oxidative phosphorylation
6.Sources and function of Vitamin D
7.Protein calorie malnutrition Write briefly: 5X2=10
8.Absorption of Vitamin B-12
9.Causes of fatty liver
10.Clinical applications of competitive inhibilitior
11.Proenzymes and their diagnostic importance

12.Functions of
phospholipids-----------------------------------------------------------------------------------------------------
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BIO-CHEMISTRY FIRST YEAR-SEPT/OCT .2005 NEW REGULATIONS 500-B
1.Explain the process of translation under the following headings a) activation of

aminoacid b) intitiation c) elongation d)termination e) post-translational processing.
(2+2+2+2+2=10)
2.Name body buffers. Explain how acid base balance is maintained in the body. Give the
normal levels of Sodium, Potassium, Chloride, Bicarbonate in the blood. (1+7+2=10) Write
short notes on: (5x4=20)
3.Secondary structure of proteins
4. Fluid mosaic model
5.Serum calcium homeostasis
6.DNA repair,machanisms
7.Glucocorticoids
Write briefly on. (5x2=10)
8. Name clearance tests used to assess kindney function.
9.Anticancer agents
10.compare and contrast DNA with RNA
11.Genetic code
12.Mention the biochemical defect in
a) Hemocystinuria b) Parkinsonism
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BIO-CHEMISTRY FIRST YEAR-APRIL .2006 NEW REGULATIONS 500-A
1.write source,chemistry, recommended dietary allowances

absorption,functions and deficiency manifestations of folic acid.
(1+1+1+1+4+2=10)
2.Describe the reactions of Pontose phosphate pathway indicating the sites
and significance. Add anete on glucose-6-phosphate dehydrogenase
deficiency. (5+2+2+1=10)
3.Schematically represent the ETC (Electron Transport chain) indicating the
sites of ATP generation and inhibitors.
4. Mention the biologically important nucleotide coenzymes and their
functions.
5. Congenital hyperbilirubinaemias.
6.Name the different types of lipases.Mention their mechanism of activation,
site of action and functions.
7.Measures of dietary protein quality.
8. What is carnitine and its function,
9.Mention two abnormal hemoglobins and how do they differ from normal
adult Hb.
10.Zellwegers syndrome.
11.What is biotransformation? Give two example.
12. Aldolase B

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BIO-CHEMISTRY FIRST YEAR-APRIL .2006 NEW REGULATIONS 500-B
1.Write the sources,daily rejpuirements, factors affecting absorption and biochemical

functions of Iron in the body. And add a note on altered Iron metabolism. (1+1+2+4+2=10)
2. what is active methionine ? How it is formed ? What are its functions ? Explain the steps
of methionine metabolism. Write the disorders of its metabolism. (1+1+2+4+2=10)
3.Structure and function of MRA.
4.Chromatography.
5. List the Liver Function Tests. Explain the application of LFT in diagnosis of different
types of jaundice.
6.Name the plasma proteins. Mention the normal ranges and funcstions of each.
7.Mechanisms of renal regulation of Ph.
8.Isoelecstric PH of renal regulation of PH.
9.what is the normal range of Serum Potassium? What are the clinical manifestations of
hypokalaemia?
10.write the functions of enkaryotic RNA polymerases.
11.what are oncogenes and their significance?
12.what are restriction endonucleases ? Give 2 examples.

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BIO-CHEMISTRY FIRST YEAR-SEPT .2006 500-A
What are enzymes and proenzymes ? Mention diagnostic importance of

proenzymes. Classify enzymes giving examples of each class. Indicate the
reaction catalysed by the enzyme in each class. (2+2+3+3=10)
Glycogenesis and Glycogenolysis . explain the relations involved in
Glycogenesis and Glycogenolysis in the liver. How are these two pathways
reciprocally regulated ? Name glycogen storage diseases. (1+4+3+2=10)
De novo synthesis of fatty acids.

Functions and sources of Vitamin C.
Hemoglobinopathies.
Basal Metabolic Rate.
Electron Transport chain.
8.Deficiency manifestations and Biochemical Role of Vitamin E.
9. Unsaturated fatty acids.

10. detoxification by hydrolysis.
11.lactose intolerance.
12.Oxidative phosphorylation and Substrate le phosphorylation and substrate le

phosphorylation.
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BIO-CHEMISTRY FIRST YEAR-SEPT .2006 -500-B
Define proteins. Explain structural organization of proteins. Add anote

on denaturation. (1+7+2=10)
Explain the iron metabolism under the following headings:
Sources b) Daily requirements c) Absorption and Transport
d) Functions e) Clinical Abnormality (1+1+3+3+2=10)
Role of kindney in acid base regulation.

De novo purine synthesis.
Types of RNAs and their functions.
Mechanism of action of steroid hormones.
Structure and functions of Immunoglobulin E (IgE)
Creatinine clearance and its significance.

Write four structural features of cell membrane.
Define oncogene and protooncogene.
Write four applications of Recombinant DNA technology.
Name electrolytes. Mention their normal serum level.

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BIO-CHEMISTRY FIRST YEAR-APRIL/MAY .2007 NEW -500-A
Explain how palnuitic acid is oxidized in our body ? How much energy is
liverated. How acetyl Coa.level is regulated. (6+2+2=10)
What are the fates of glucose-6-phosphate? Explain HMP shunt pathway and
state its significance. (2+5+3=10)

Name the coenzymes of Nlacin and thramine and give two metabolic
functions of each.
Schematic representation of electron transport chain.
5. Fuctions of cholesteroj
6. Porphyria
7.Factoze
8.Uncouplers of oxidative phosphoryletion
9. enzyme markers in myocardial infarction,
10. factors influencing biological value of proteins.
11. .The post-transcriptional modification ofRNAs
12.dietary requirement and and defiency manifestations of Vitamin A.
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BIO-CHEMISTRY FIRST YEAR-MAY .2007 500-B

Explain the formation of uric acid. What is the normal serum uric acid level ?
explain the disease associated with its accumulation. Suggest a way for
lowering serum uric acid level. (4+1+3+2=10)
Enumerate kidney function tests and liver function test. Give a detail account
on one kidney function test and one liver function test. (2+2+3+3=10)
Urea cycle
Metabolic Acidosis and alkalosis
Sources and functions of copper
Functions of plasma proteins
Salient features of the genetic cod
Write Breifly on : (5x2=10)
Apoptosis
Gene library
Fates of glycine
Homocystinuria
Oxytocin

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BIO-CHEMISTRY FIRST YEAR-SEP/OCT .2007 500-A
1.Define "glycogenesis" abd "glycogenolysis". Name the conditions in which ketosis occurs.
Describe the synthesis and catabolism of ketone bodies. How do you test for ketone
bodies. How do you test for ketone bodies in urine? (2+5+3=10)
2. explain the terms "ketonemia" and "ketosis". Name the conditions in which ketosis
occurs. Describe the synthesis and catabolism of ketone bodies. How do you test for ketone
bodies in urine? (2+1+6+1=10)
3. biolaogical value of proteins
4. sickle cell haemoglobin
5. rickets
6. detoxification by conjugation
7. von Gierks Disease
Uncouplers of oxidative phosphorylation

Effect pf temperature on enzyme activity
Zymogens
Define Epimer. Name two epimers
Mention the importance of phosphotidy inositol.
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BIO-CHEMISTRY FIRST YEAR-SEP/OCT .2007 500-B
Desribe in nitrogenous bases present in the nucleic acids with suitable

example. Mention the source of each of the atoms present in the purine ring.
Describe the catabolism of purine nucleotides disorders. (8+2=10)
Classify the nitrogenous bases present in the nucleic acids with suitable
example. Mention the source of each of the atoms present in the purine ring.
Describe the catabolism of purine nucleotides. Write briefly on the associated
metabolic disorders. (2+2+4+2=10)
Creatinine clearance
Genetic code
Facilitated diffusion
Regulation of serum calcium level
Respiratory acids
Non-protein amino acids

Biochemical function of selenium
Name two biologically important nucleotides and mention their functions.
Menkes disease
Phosphoadenosine phosphosulphate(PAPS)
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BIO-CHEMISTRY FIRST YEAR-MARCH/APRIL .2008 500-A
What are ketone bodies? How are they synthesized? Name the conditions
characterized by excessive production of ketone (1+3+1+5=10)
What are the metabolic fates of glucose-6-phosphate? Explain HMP shunt
pathway and mention its significance. (2+6+2=10)
What is competitive inhibition? Write its clinical applications.

High energy compounds
Porphyrias
Biochemical functions and deficiency manifestations of folic acid
Calorificvalue
Essential fatty acids

Redox potential
Sources and deficiency manifestations of vitamin A
Detoxification by hydrolysis(two examples)
Composition and importance of Insulin.
BIO-CHEMISTRY FIRST YEAR-MARCH/APRIL .2008 500-B
Name aromatic amino acids. Give an account on the metabolism of tyrosine.

What are the biologically important compounds derived from tyrosine?
Which are the inborn errors associated with this amino acid?
Give an account of the sources, absorption, requirement, functions and
regulations of calcium.
Induction and repression

Structure and function of RNA
Respiratory and metabolic acidosis
Gout
Name four different types of nucleotides and mention their biological
importance
Tumor markers
Structural features of cell membrance
Urea clearance
Define mutagens and give two examples
hybridoma
BIO-CHEMISTRY FIRST YEAR-JULY .2008 -500-A
Explain how palmitic acid is oxidized in our body. How much energy is
released? Explain how acetyl coa level is regulated? (6+2+2=10)
What are enzymes? Classify them with examples. Give an account on the
effect of substrate concentration, ph and temperature on enzyme action.
Explain the significance of Km and Vmax. (1+3+3+3=10)

3.steps of glycogenesis and its significance.
4. P:O ratio and respiratory control.
5. Hormonal regulation of blood glucose.
6. vitamin E
7. abnormalities associated with billirubin metabolism. Write Breifly on : (5x2=10)
8. lactose.
9. How Aspirin and Indole undergo biotransformation?

10. Specific dynamic action of food.
11. Rapport lube ring cycle.
12. cobalamin-functions and deficiency manifestations
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BIO-CHEMISTRY FIRST YEAR-FEBRUARY.2009 -500-A
Describe tricarboxylic acid cycle with its energetic and inhibitors. Add a note
on anaplerotic reactions. (6+2+2=10)
Describe Hemoglobin structure,functions and metabolism. Write brief on
porphyrias and mention any two laboratory tests to diagnose them.
(5+3+2=10)
Isoenzymes and their clinical importance.

Glycosaminoglycans and their functions
Define basal metabolic rate(BMR) and list the factors affecting BMR.6.
Synthesis and functions of Calcitrik.
Classify phospholipids and mention their functions.
Sources and functions of folic acid.

Biomedical importance of prostaglandins
Name the bile salts and mention their functions
What is carnitine and its role in oxidation of fatty acids
Give examples of uncouplers and Inhibitors of oxidative phosphorylation

BIO-CHEMISTRY FIRST YEAR-FEBRUARY.2009 -500-B
Write the sources, daily requirement, factors affecting the absorption and
functions of calcium. Add a note on hormonal regulation of serum calcium.
Discuss the sources of ammonia in the body and explain how it is detoxified.
Mention normal range of blood ammonia and list the causes of ammonia
intoxication.
Mutations
Biochemical actions of Insulin
Gastic function Tests.
Serum protein electrophoresis
Catabolism of purines
Anion gap and its significance

Phenylketonuria
Tumor markers
Active Transport
Xeroderma pigmentosum.
BIO-CHEMISTRY FIRST YEAR-JULY.2009 -500-A

Discuss the metabolism of ketone bodies and add a note on ketosis. Write
briefly on the tests done for the detection of ketone bodies in urine. (7+3=10)
Write the steps of HMP SHUNT pathway. Write the significance of this
pathway (7+3=10)
Specificity of enzymes.
High energy compounds with examples.
What are porphyrias? Write examples.
Functions and deficiency manifestations of Vitamin A.
Fatty acid synthase complex
Name the enzyme deficit in the following conditions

Galoctosemia b) Nieman picks Disease
Specific Dynamic Action.
Anti vitamins
Structure of sucrose.
Mechanisms of Detoxification.
BIO-CHEMISTRY FIRST YEAR-JULY.2009 -500-B

How is ammonia detoxified in the body? Give an account of the urea cycle.
Add a note on the enzyme defects in the cycle. (2+6+2=10)
Explain the steps involved in the synthesis of Recombinant DNA. Mention
the clinical applications of this technique. (7+3=10)
Metabolic acidosis
Functions and deficiency manifestations of calcium.
Primary structure of protenins.
Mechanism of action of steroid hormones.
Hepatic functional tests
Wilsons Disease.
Write the normal serum levels of
Sodium b) potassium c) creatinine d) urea
Hartnups disease.
Anticancer agents.
Write the general structure of immunoglobulins.
BIO-CHEMISTRY FIRST YEAR-JANUARY.2010-500-A

Outline the reactions of Hexose Monophosphate Shunt pathway. In which

tissues this pathway is operative? What is the significance of this pathway?
(6+2+2=10)
How is NADH oxidized in the respiratory chain? Indicate the sites of
oxidative phosphorylation. What is chemiosmotic theory? (4+3+3=10)
Functions and deficiency of Niacin
Pyruvate dehydrogenase complex
Phospholipids and their functions
Glycogen storage diseases
Detoxification by conjugation
Functions of high density lipoprotein

Biochemically important compounds derived
Proenzymes and their importance
What are ligases? Give two examples
Functions of ascorbic acid

------------------------------------------------------------------------------------------------------------ QUESTI
ON PAPERS-M.B.B.S
BIO-CHEMISTRY FIRST YEAR-JANUARY.2010-500-B

How is phenylalanine converted to tyrosine in the body? What is

phenylketonuria? Outline the formation of thyroid hormones and
catecholamines from tyrosine. (2+2+3+3=10)
Gine and account of Watson-Crick model of DNA. List the differences
between DNA and RNA. How is DNA replicated? (4+2+4=10)
Biochemical functions of copper.

Clearance Tests.
Characteristics of genetic code.
Paper Electrophoresis.
Metabolic acidosis
Definition and forces responsible for tertiary

Name four important substances derived from glycine
Name any two gastrointestinal hormones. What is their mechanism of action?
Functions of plasma Albumin
What do you mean by post translational
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QUESTIONPAPERS-M.B.B.S
BIO-CHEMISTRY FIRST YEAR-JULY.2010-500-A
Explain the formation, utilization and excretion of ketone bodies. What is

ketoacidosis?(4+2+2+2=10)
How is acetyl CoA oxidized in citric acid cycle? What is its energetic? Why it
is called amphibolic pathway? (6+2+2=10)
Isoenzymes
Fatty liver
Inhibitors of respiratory chain
Diagnostic importance of enzymes
Biochemical functions of Vitamin D
Cori cycle
Hyaluronic acid and its functions
What is substrate level phosphorylation? Give two examples
Functions of cholesterol
What are lyases? Give two examples.

------------------------------------------------------------------------------------------------------------ BIO-
CHEMISTRY FIRST YEAR-JULY.2010-500-B
How is glycine degraded in the body? Outline the synthesis of creatine from
glycine. Enumerate the metabolic diseases of glycine (4+3+3=10)
Explain transcription. Name the different types of RNA and indicate their
functions (6+2+2=10)
Biochemical functions of zinc and iodine

Nitrogen balance
Blood buffers and regulation of pH
Biologically active peptides
Recombinant DNA and its applications
8.what is isoelectric pH of a protein? Mention two properties of a protein at this Ph
9. what is creatine clearance? What is its diagnostic importance?
10. Name any two Group I hormones. What is their mechanism of action?
11. write the functions of immunoglobulin G.
12. What are tumor markers? Give two examples.

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Describe the sources, dietary requirements,biochemical functions and

deficiency manifestations of Vitamin A (1+1+4+4=10)
Mention the pathways by which Glucose is metabolized in the body. Describe
the steps of anaerobic glycloysis and its energetic. (2+6+2=10)
Schematically represent the Electron Transport chain indicating the sites of

ATP production and Inhibitors.
Formation and fate of Bile pigments.
Factors affecting enzyme activity.
Abnormal Hemoglobins
Lipoproteins.

Biological value of proteins.
Km value and its significance
Dietary fiber.
Detoxification by oxidation
Lactose intolerance
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Define a buffer. Explain the various mechanisms of regulation of acid-base

balance. Add a note on acid-base balance. Add a note on acid-base disorders
(1+7+2=10)
Describe the steps of eukaryotic replication of DNA. Add a note on Reverse
transcription
Absorption and transportation of Iron

Purine salvage pathways.
Outline the steps of biosynthesis of Urea.
Mechanisms of hormone action
Renal function tests.
Define denaturation of proteins. Give examples of denaturing agents

What are plasma proteins and write their normal ranges?
What are oncogenes and give examples?
Orotic acidurias
Mention the biochemical defects in:-
Alkaptonuria b) maple syrup urine disease

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Describe the CITRIC ACID cycle with energetic. Explain the Amphibolic role
of this cycle? (6+2+2)
Write the sources,daily repuirement, finctions and deficiency manifestations
of Vitamin C (2+1+4+3=10)

Chemiosmotic theory and oxidative phosphorylation
Porphyrias
Digestion and absorption of lipids.
Competitive Inhibition and its clinical significance
Enzyme markers in myocardial infarction.
give two examples for phospholipids and write their functions

Specific dynamic action.
Specific Dynamic Action
MUTAROTATION
What are Antivitamins? Give any two examples with vitamin inhibited by
them
Absolute specificity of enzymes.

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Define a buffer. Explain the various mechanisms of regulation of acid-base

balance. Add a note on acid-base disorders (1+7+2=10)
Describe the steps of eukaryotic replication of DNA. Add a note on reverse
transcription. (8+2=10)
Absorption and transportation of iron
Purine salvage pathways
Outline the steps of biosynthesis of urea
Mechanisms of hormone action
Renal function Tests
Define denaturation of proteins. Give examples of denaturation agents.

What are plasma proteins and write their normal ranges?
What are oncogenes and geve examples?
Orotic acidurias
Mention the biochemical defects in:
Alkaptonuria b) maple syrup urine disease
------------------------------------------------------------------------------------------------------------ QUESTI
ON PAPERS-M.B.B.S
BIO-CHEMISTRY FIRST YEAR-JULY.2011-500-A
Describe the CITIC ACID cycle with energetic . explain the Amphibolic role
of this cycle? (6+2+2=10)
Write the sources, daily repuirements, functions and deficiency
manifestations of vitamin C? (2+1+4+3=10)
Chemiosmotic theory and oxidative phosphorylation

Porphyrias
Digestion and absorption of lipids
Competitive Inhibition and its clinical significance
Enzyme markers in myocardial infarction
Give two examples for phospholipids and write their functions

Specific dynamic action
Mutarotation
What are antivitamins? Give any two examples with vitamin inhibited by
them
Absolute specificity of enzymes.

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BIO-CHEMISTRY FIRST YEAR-JULY.2011-500-B

What is the normal Ph of blood? Discuss the respiratory and renal regulation
of Ph? (1+4+5=10)
Explain the pathway of catabolism of Tyrosine. Write the important products
synthesized from tyrosine. Add a note on albinism. (5+3+2=10)
Replication
Fluid mosaic model of membrane structure.
What is Replication DNA? What is the role of restriction endonuclease in
Recombinant DNA technique?
Name the plasma proteins. List any four functions of them in the human
body
Creatinine clearance test.
Apoptosis
Oxytocin
Fluorosis
Vandenbergs Test
Anion gap

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Explain the various factors affecting the enzyme activity. Add a note
on the significance of the km value of the enzyme
Discuss the mitochondrial electron transport chain (E.T.C) and the
inhibitors at various sites of this chain
Detoxification by conjugation
Glycogen storage diseases.
Fatty liver and lipotropic factors
Hemoglobinopathies with examples
Functions and deficiency features of pyridoxine
Define isoenzymes. Give two examples and their diagnostic use.

Functions of bile Salts
Energetics of TCA (tricarboxylic acid) cycle.
Define antioxidants. Which vitamins have antioxidant function?
Respiratory quotient.

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Describe the steps of transcription in Eukaryotes. Give two examples

for post transcriptional modifications (8+2=10)
Discuss the metabolism of calcium under the following sections:
Sources b) recommended daily allowance c) functions (any 4) d)
Regulation of plasma level e) deficiency manifestations
(1+1+4+2+2=10)
Plasma buffers and the role of buffers in the regulation of Ph

Mechanisms of action of hormones.
Active transport with 2 examples
Biological important products derived from glycine.
Enumerate the liver function tests. Explain the detoxification of
bilirubin by the liver.
Role of copper in iron metabolism

Orotic aciduria
Bonds responsible for maintaining the higher levels
Ribozymes
Oncofetal antigens

Ntruhs Biochemistry

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BIOCHEMISTRY NTRUHS PREVIOUS QUESTION PAPERS

BIO-CHEMISTRY FIRST YEAR-APRIL .2004 NEW REGULATIONS -500-A

ANSWER ALL QUESTIONS

1.Explain the chemistry,daily allowance,sources,metabolic role and deficiency diseases

Write short notes on: (5X4=20)

3.Prostaglandlns and their functions.

4.Inhibaitors and electron transport chain.

5.Factors influencing enzyme activity.

8.Essential fatty acids(efa) (5X2=10)

11.Defiency of Glucose-6-phosphate dehydrogenase.

b)Serum acid phosphatase

BIO-CHEMISTRY FIRST YEAR-APRIL .2004 NEW REGULATIONS 500-b

Write short notes on: (5X4=20)

3.i RN and its functions.

5.Renal functions tests.

7.biological role of fluorine in the body.

Write briefly on: (5x2=10)

11.Biochemical findings in blood and urine in obstructine jaundice.

BIO-CHEMISTRY FIRST YEAR-OCT .2004 NEW REGULATIONS 500-A

1.Define Gluconeogenesis explain the pathway in humans from its predominant

3.structural composition and functions of lipoproteins.

4.enzyme inhibitors and their clinical uses.

5.deficiency manifestations of pyridoxine.

6.Boyers binding change mechanism of ATP synthesis.

7.mechanisms of absorption of sugars from the gut.

8.a) BMR and its normol values (5x2=10)

b) Net protein utilization

9.The enzymes defective in

10.cardiolipin and its clinical significance.

11."High energy" compound with four examples.

12.Biotransformation with 2 examples.

ANSWER ALL QUESTIONS

3.Re plic ation of DNA

4.Deficiency disorders of iodinc

5.the plasma proteins mentioning their normal ranges and functions

6. Purinc salvage pathways

7.Renal function tests

8The enzyme and coenzyme required in the conversion of: (5x2=10)

a)Glycine to serinc . b )3-HYdroxy kynurenine to 3- b Hydroxy anthanilate

9. Biochemical defects in:

a)Cystiosis b)Hartnups disease

11.The post-transcriptional modification of RNAs.

12.Mechanisms of actions of insulin.

BIO-CHEMISTRY FIRST YEAR-MARCH/APRIL .2005 NEW REGULATIONS 500-A

MAX.MARKS:50 PAPER-1 TIME:2.30 HOURS

ANSWER ALL QUESTIONS

write short notes on: (5x4=20)

3.clinical significance of isoenzymes.

5.Acute intermittent porphyria.

6.Specific Dynamic ac tion of food.

Write briefly: 5X2=10

11.Name four esssntial amino acids

12.Mention the normal plasma values of the fallowing electrolytes:

a)Serum Sodium b)Serum potassium

c)Serum Calcium d)Serum Chloride

BIO-CHEMISTRY FIRST YEAR-APRIL .2005 NEW REGULATIONS 500-B

MAX.MARKS:50 PAPER-2 TIME:2.30 HOURS

ANSWER ALL QUESTIONS.

WRITE Short notes on: (5X4=20)

3. Secondary structure ofproteins

4. Fluid Mosaic model

5. Serum calcium homeostasis

6 .DNA repair mechanisms

10. Compare and contrast DNA withRNA