Syllabus of Biochemistry (including medical physics and
molecular biology) for first professional MBBS students of the University of Health Sciences.
Departmental objective:
Knowledge:
At the end of the course the
student will be able to -
1) Describe the molecular and
functional organization of a cell and list its subcellular components.
2) Delineate structure ,
function and interrelationship of biomolecules and consequences of deviation
from the normal.
3) Summarize the fundamental
aspects of enzymology and clinical application wherein regulation of enzyme
activity is altered
4) Describe digestion and
assimilation of nutrients and consequently or malnutrition consequences of
malnutrition.
5) Integrate the various aspects
of metabolism and their regulatory pathways.
6) Explain the biochemical basis
of inherited disorders with their associated sequelae.
7) Describe mechanisms involved
in maintainance of body fluids and p H homeostasis.
8) Outline the molecular
mechanisms of gene expression and regulations of the principles of genetic
engineering and their application in medicine
9) Summerise molecular concept
of body defences and their applicaton in medicine
10) Outline the biochemical
basis of environmental health hazards, biochemical basis of cancer and carcinogenesis
11) Familiarize with the
principles of various conventional and specialized laboratory investigations
and interpretation of a given data.
12) Suggest experiments to
support theoretical concepts and clinical diagnosis.
PROPOSED SYLLABUS OF BIOCHEMISTRY FOR FIRST PROFESSIONAL
M.B.B.S COURSE
No.of Theory:
144 hrs.
Lectures/tutorials: GENERAL REVIEW
1) Origin of life . Molecular
logic of living matters .Why biochemistry has been included in the medical
curriculum.
2) A review of cellular structure
and functions in chemical terms ; Special reference to separation of
subcellular fractions and their identification.
3) Simple building blocks ;
organization of macromolecules.
CHEMISTRY OF LIVING MATTERS
4) Carbohydrates : its nomenclature , classification with
examples chemical structures of monosaccharides and disaccharides in pyranose
and furanose form.
5) Isomerism : stereoisomers , optical isomers , epimers ,
anomers .Mutarotation, specific rotation.
6) Glycosidic linkage ; deoxy and amino sugars and
homopolysaccharides, their chemical structures and importance.
7) Chemical structures of heteropolysaccharides ,
glycosaminoglycans and glycoproteins.
8) Carbohydrates in bacterial cell wall and blood group
substances.
9) Interpretation of chemical reactions of carbohydrates.
10)Classification of lipids .Chemical structure of simple
lipids .Nomenclature of saturated and unsaturated fatty acids.
11) Essential fatty acids ; Importance of omega 3 fatty acids
; structure and functions of prostaglandins, leucotrienes and thromboxanes.
12) Classification and structure of phospholipids .Surfactant
.Glycolipids.
13) Derived lipids : structure of cholesterol, steroid
hormones , bile acids.
14) Characterisation of lipids: Saponification no. Iodine no.
Acid no. Acetyl no. Polensky no. R.M. no. Thin layer chromatography , gas
liquid chromatography
15) Proteins : Classification, chemical and physical
properties
16)Bonds maintaining protein structure , organization of
protein structure, alpha helix and beta pleated sheath .Globular proteins and
fibrous proteins.
17) Classification and chemical structures of amino acids
18) Chemical reactions of amino acids ; Isoelectric pH , acid
base properties of amino acids.
19) Methods of protein separation ; Gel filtration , electrophoresis
ultracentrifugation.
20) Determination of primary structure of proteins .Ninhydrin
reaction.
21) Separation of amino acids ; Paper chromatography , Thin
layer chromatography, High performance liquid chromatography , SDS
polyacrylamide gel electrophoresis.
22 & 23) Classification and structure of immunoglobulins
and other plasma proteins.
24,25 & 26) Structure , function and relationship of a
protein : Haemoglobin and myoglobin ;Role of 2,3 DPG , Hb S ,Hb M ,
Thalassemia.
27& 28) Structure ,function and relationship of a protein
: Collagen , Keratin
Fibrin and Elastin.
29) Chemical structure of Purine , Pyrimidine ,Nucleoside
,Nucleotide and
derived nucleotides
30) Structures and properties of DNA in different forms.
31) Structures and properties of m-RNA ,t- RNA ,r-RNA and
hn-RNA.
ENZYMES
32) I.U.B. classification of enzymes with examples .Apoenzyme
, coenzyme, holoenzyme and cofactors
33) Kinetics of enzymes :
Reaction velocity, order of reaction, specific activity,
Michaelis-Menten equation .Significance
of Km.
34) Factors affecting enzymatic
activity : temperature , pH , substrate
concentration and enzyme
concentration.
35) Inhibitors of enzyme action
: Competitive , non- competitive, irreversible
and suicidal . Lineweaber — Burk
plot.
36) Enzyme : Mode of action,
allosteric and covalent regulation.
37) Functional and nonfunctional
enzymes . Clinical significance of enzymes
38) Measurement of enzyme
activity and interpretation of units. Measurement
with coupled reactions.
39) Isozymes : Properties ,
measurement and significance
40) Principles of enzyme linked
immunosorbent assay (ELISA).
PHYSICAL ASPECTS OF LIVING MATTERS
41) Isotopes , radioisotopes ,
ionizing radiations , Radioimmunoassay.
42) Colloid, crystalloid,
osmotic pressure and colloidal osmotic pressure.
43) Acid, base and Ph:
Definition, Hendersan —Hasselbach equation.
44) Buffer: Definition , types
and mechanism of action
45) Laws of thermodynamics ,
redox potential , free energy , high energy bonds.
46) Biological oxidation:
Enzymes involved , generation of superoxide free radicals , role of cytochrome
P450.
47) Components of mitochondrial
respiratory chain , its organization and function .Sites of ATP formation,
inhibitors and uncouplers.
48) Mechanism of oxidative
phosphorylation, inhibitors , ATP/ADP cycle.
49) Shuttle mechanism :
Glycerophosphate shuttle , Malate shuttle and creatine phosphate shuttle.
50) Mechanism of transport or
absorption across a biomembrane : Active passive , facilitated transport and
endocytosis.
51) Information transfer through
a biomembrane : Role of G proteins and c AMP, phophatidylinositol pathway.
METABOLISM
52) Metabolism : An overview .
Control of a metabolic pathway.
53) Methods of study.
54) Mechanism of hormone action.
METABOLISM OF CARBOHYDRATES
55) Digestion and absorption of
carbohydrates . Lactose intolerance.
56,57 & 58 ) Fate of glucose
after absorption . Glycolytic pathway: Chemical
structures of intermediates ,
allosteric control of key enzymes , inhibitors
energy production and hormonal
control.
59,60) Glycogenesis and
Glycogenolysis : Covalent modification of enzymes,
hormonal control ,glycogen
storage disease
61) Conversion of Pyruvate to
Acetyl coA .Control of Pyruvate
dehydrogenase complex.
62, 63 & 64) Tricarboxilic
acid cycle : Chemical structure of intermediates
sites of ATP production,
regulatory mechanism.
65) Normal and abnormal
metabolism of Fructose and Galactose.
66) Gluconeogenesis : From
Lactate , Glycerol and Glucogenic amino acids
Control of key gluconeogenetic
enzymes.
67) Pentose phosphate pathway :
Importance of generation of NADPH
Glutathione and red cell
membrane integrity.
68) Formation of Glucuronic acid
and its significance. Its structural resemblance
with Ascorbic acid.
69 & 70) Glucose tolerance
test: oral and intravenous. Procedure and
interpretation. Glycosuria,
glycosylated hemoglobin.
METABOLISM OF LIPIDS
71) Digestion and absorption of
fats: Micelle formation. Reconstitution of lipid in
mucosal cell. Role of bile and
pancreatic secretion.
72) Transport of lipids:
Classification of lipoproteins, their chemical structure,
composition; apoproteins.
73 &74) Metabolism of
chylomicrons, VLDL, LDL, HDL; disorders of lipoprotein
metabolism.
75) Oxidation of fatty acids
(alpha, beta, and omega): saturated and unsaturated;
odd carbon atom and even carbon
atom fatty acids. Role of Carnitine.
76) Energetic and disorders of
fatty acid oxidation.
77) Formation and degradation of
ketone bodies, ketosis.
78) Metabolism of lipids in
liver; causes and prevention of fatty liver, lipotropic
factors.
79) Metabolism of lipids in
adipose tissues and its hormonal controls.
80 & 81) Biosynthesis of
fatty acids: De novo and on existing primer chain.
Process of chain elongation.
Detailed action of Biotin; multienzyme complex
concept.
82 & 83) Biosynthesis of
cholesterol: metabolic steps, control of rate limiting
steps. Cholesterol lowering
drugs: their mechanism of action.
84 &85) Formation of bile
acids and steroid hormones. Biosynthesis of
Triacylglycerol and
Phospholipids and its degradation.
86, 87, & 88) chemical
structure, synthesis, secretion, transport and degradation of
insulin, mechanism of action.
Insulin receptors. Insulin like growth factors.
89) Structure and mechanism of
action of Glucagon.
METABOLISM OF PROTEINS
90) Dietary protein, its
biological value and digestibility coefficient .Protein
malnutrition . Essential amino
acids.
91) Digestion of proteins;
absorption of amino acids , gama- glutamyl cycle.
92) Fate of amino acid after absorption . Process of
transamination : Role of Pyridoxal phosphate.
93) Oxidative and nonoxidative
deamination , decarboxylation and transmethylation .Formation of Creatinine.
94) Formation and disposal of
ammonia . Urea formation . Disorders of Urea cycle . Formation of Nitric oxide.
95 & 96) Normal and abnormal metabolism of
Phenylalanine and Tyrosine
Formation of Melanin. Formation
and degradation of Catecholamines.
97) Normal and abnormal
metabolism of sulphur containing amino acids.
98) Normal and abnormal
metabolism of Tryptophan.
99) Normal and abnormal
metabolism of Histidine. Inborn errors of metabolism in
relation to protein metabolism.
100) Synthesis of Haem .
Chemistry of porphyrins . Enzymatic defects in Porphyria.
l01& 102) Degradation of
Haem . Conjugated and unconjugated hyperbilirubinaemia
103) Biochemical mechanism of
blood coagulation.
METABOLISM OF INORGANIC ELEMENTS AND VITAMINS
104 & 105) Metabolism of
Iron : dietary source, digestion, absorption ,transport
utilization and storage.
106& 107) Normal
and abnormal metabolism of Calcium and Phosphorous Dietary source, digestion,
absorption, transport, utilization and excretion. Mechanism of bone formation.
108) Chemical structure and
synthesis of Vitamin D. Its hormone like action on
Calcium and Phosphorous
metabolism.
109& 110) Chemical
structure,synthesis and degradation of Parathyroid hormone.
Its action on Calcium and
Phosphorous metabolism.
111) Role of micronutrient e.g.
Zinc and Selenium in the body.
11 2& 113) Composition of
intracellular and extracellular compartment fluid
.Water and Sodium balance . Role
of kidney in its maintainance.
114) Respiratory and renal
mechanism for pH regulation.
115) Disorders of acid base
balance and its compensation; Anion gap.
116) Chemistry and action of
Vitamin A, Hypervitaminosis . Role of Retinoic acid.
117) Chemistry of Vitamin E; its
action as an antioxidant.
118) Chemistry and function of
Vitamin K.
119) Chemistry and function of
Folic acid and Vitamin B 12 in one carbon metabolism.
120) Chemistry and function of
riboflavin, pantothenate, and nicotinamide.
FUNCTIONAL TESTS
124) Renal clearance tests.
1 Liver function tests.
123) Thyroid function tests.
124) Gastric and Pancreatic
function tests.
METABOLISM OF PUTRINE AND PYRIMIDINE
125) Source of carbon and
nitrogen in the synthesis of purine and pyrimidine.
Purine salvage pathway.
126) Catabolism of purine and
pyrimidine.
127) Disorders of purine and
pyrimidine metabolism.
GENETIC ASPECTS
128) Gene: mutation, genetic
code.
129) Regulation of gene
expression: Lac-Operon and His-Operon model. Role of
histone and non histone
proteins.
130) Replication of DNA.
Difference between eukaryoric and prokaryotic DNA
polymerase. DNA repair
mechanism.
131 & 132) Role of different
forms of RNA. Process of transcription, RNA
repication, post transcriptional
modification.
133 & 134) Steps of protein
biosynrhesis in Eukatyotes and Prokaryotes.
Posttranslational modification
of protein.
135) Inhibitors of DNA, RNA and
protein synthesis.
136) Genome of Retrovirus; Cell
cycle, Apoptosis.
CANCER AND XENOBIOTICS
137&138) Biochemistry of
cancer: chemical and physical carcinogens, Oncogenes and Proto-oncogenes.
139 & 140) Metabolism of
Xenobiotics: different types, detoxification, and its impact on the body.
GENETIC METHODOLOGY
141) RFLP AND \TNTR: Explanation
and their application in medicine.
142) Principles of Southern
blotting, Northern blotting and Western blotting, and
their application in biology and
medicine.
143) Steps of cDNA synthesis in
vitro. Principles of recombinant DNA technology.
144) Principles of polymerase chain reaction, concept of
genomic library and its application.
125) Source of carbon and
nitrogen in the synthesis of purine and pyrimidine.
Purine salvage pathway.
126) Catabolism of purine and
pyrimidine.
127) Disorders of purine and
pyrimidine metabolism.
GENETIC ASPECTS
128)
Gene: mutation, genetic code.
129) Regulation of gene
expression: Lac-Operon and His-Operon model. Role of histone and non histone
proteins.
130)
Replication of DNA. Difference between eukaryoric and prokaryotic DNA
polymerase.
DNA repair mechanism.
131
&132) Role of different forms of RNA. Process of transcription, RNA
replcation,
post transcriptional modification.
133
& 134) Steps of protein biosynrhesis in Eukatyotes and Prokaryotes.
Posttranslational
modification of protein.
135)
Inhibitors of DNA, RNA and protein synthesis.
136) Genome of Retrovirus; Cell
cycle, Apoptosis.
CANCER AND XENOBIOTICS
137&138) Biochemistry of
cancer: chemical and physical carcinogens, Oncogenes and Proto-oncogenes.
139 & 140) Metabolism of
Xenobiotics: different types, detoxification, and its impact on the body.
GENETIC METHODOLOGY
141) RFLP AND VNTR: Explanation
and their application in medicine.
142) Principles of Southern blotting, Northern
blotting and Western blotting, and their application in biology and medicine.
143) Steps of cDNA synthesis in
vitro. Principles of recombinant DNA technology.
144) Principles of polymerase
chain reaction, concept of genomic library and its application.
SKILL DEVELOPMENT (Practical): 80
hours.
LESSON 1-4: Monosaccharides
(glucose, fructose), disaccharides (lactose, sucrose), polysaccharides (starch,
dextrin).
LESSON 5-6: Identification of
any one of the unknown carbohydrates.
LESSON 7-8: Identification of simple protein (egg albumin) by
following colour reaction:
Biuret test, Millon’s test,
Xanthoproteic test.
LESSON 9-10: Identification of
simple protein by heat and acid coagulation reaction;
Identification of simple protein
by Esbach’s precipitation reaction;
Identification of derived
protein (gelatin and peptone) by the above mentioned reaction.
LESSON 11: Identification of
glycerol by acrolein test.
To perform the experiment with
cholesterol crystal to test solubility and reaction of cholesterol dissolved in
chloroform with sulfuric acid.
LESSON 12 & 13:
Identification of presence of following pathological constituents in urine
(albumin, sugar, bile salt, bile pigment, ketone body, blood).
LESSON 14&15: To perform the
experiment to verif Lambert Beer law, handling of a colorimeter.
LESSON 16-19: To perform
colorimetric estimation of blood sugar (Folin-Wu method or glucose oxidase
method).
LESSON 20-23: To perform
colorimetric estimation of blood urea (DAM method).
LESSON 24&25) To perform
colorimetric estimatio of total protein (Biuret method).
LESSON 26&27: To perform
colorimetric estimation of serum creatinine (Modified Folin-Wu alkaline picrate
method).
Interpretation of the different
biochemical data of blood and urine.
LESSON 28: To diagnose the case
of chronic renal failure.
LESSON 29) To diagnose the case
of hemolytic, hepatic, and obstructive jaundice.
LESSON 30: To diagnose the case
of hyperlipoproteinemia.
LESSON 31: To diagnose the case
of renal glycosuria.
LESSON 32: To diagnose the case
of diabetic ketoacidosis.
LESSON 33: To diagnose the case of
myocardial infarction.
LESSON 34: To diagnose the case
of starvation krtoacidosis.
LESSON 35: To diagnose the case
of acidosis (metabolic and respiratory).
LESSON 36: To diagnose the case
of alkalosis (metabolic and respiratory).
LESSON 37: To interpret the
electrophoretogram of serum protein (normal and abnormal)
LESSON 38: To determine the Rf
value of different sugar from a given paper chromatogram.
LESSON39 & 40) Acid alkali
titration: analysis of gastric acidity.
DEMONSTRATION 16
hours.
1) Amylase estimation,
2) AST&ALT,
3) Alkaline phosphatase,
4) Paper chromatography,
5) Flame photometry,
6) End point analysis vis a vis
kinetic study,
7) Thin layer chromatography,
8) Performance of a
semiautoanalyser.
Teaching hours:
Theory
(Lecture/ Tutorial): 144 hrs.
Practical : 80 hrs.
Demonstrations
: 16 hrs.
PLAN OF FIRST PROFESSIONAL MBBS EXAMINATION IN BIOCHEMISTRY
Examination will consist of two
written papers : Viva voce and Practical examination having following break up
figure marks :
1) Written papers — Two, each 50 marks.
2) Viva voce — 20 marks.
3) Practical — 40 marks
Written Papers:
Papers 1: Cell and subcellular
organelle, plasma membrane: signal transfer, chemistry of carbohydrate, lipid,
protein, nucleic acid, enzymes, acid, base and buffer (including maintenance of
acid base balance in the body), Isotopes and radioactivity, Enzymes, Digestion
and absorption of carbohydrate, Protein and lipids, Biological oxidation,
osmosis, Colloid immunological techniques (RIA, ELISP Sepaeration techniques,
Instrumentation, Functional proteins e.g. Hemoglobin, myoglobin, collagen,
alpha keratin, fibrin and elastase.
Paper II: Metabolism of
carbohydrates, lipids, proteins, purine, ptrimidine and minerals. Vitamins,
Nucleic acid and protein biostnthesis. Regulation of gene expression. Oncogenes
and tumourogenesis. Recombinant DNP technology, Xenobiotics and its metabolism.
Molecular endocrinology. Heme synthesis and degradation. Functional tests.
Note : Each paper must contain
one essay type question of 15 marks with one alternative; two modified essay
type questions each of 10 marks, out of three; five short questions
(analytical/explanatory) each of 3 marks, out of seven.
Practical :
Interpretation of charts : lOmarks,
Urine analysis : 10 marks,
Titration : 10 marks
Clinical material analysis’: 10
marks
Viva voce : 20
marks
Table - I 10 marks (Pper - I)
Table — II 10 marks (Paper — 2)
Internal assessment: 40 marks.(Theory: 20 marks,
Practical: 20 marks)
Theory: Twenty marks have been allotted.
Considering the duration of
course, continuous monthly assessment on the basis of lectures covered in each
month is advisable. Total Ten marks will be allotted for monthly assessments
which will be conducted throughout the course. On completion of the course a
test examination in the light of a final examination has to be carried out
which will also be a lpart of internal assessment. Ten marks will be allotted
for the final examination.
Practical :
The answer script of the
students who will get more than 75% mark will have to be produced at the time
of final examination to the external examiners if they so desire.
The evaluation of practical
record book will be made in the internal assessment. Marks allotted for
Practical record books is 5.
Practical examination has to be
carried out on the completion of course and 15 marks has to allotted for this
purpose.
MODEL
QUESTIONS IN BIOCHEMISTRY
FIRST
PROFESSIONAL M.B.B.S EXAMINATION
BIOCHEMISTRY
1st Paper F.M-50
1. Answer any one of the
following:
Write down the steps of
determination of the primary structure of a monomeric protein. 12
Describe the process of digestion and
absorption of triglyceride in the intestine.
12
2. Answer any two of the
following:
. Define Km and derive the rate of an enzyme
catalyzed reaction when:
[S]=Km,
[S]>>Km, [S]<<Km. 1+2+2+2
. Describe the
chemiosmotic hypothesis of oxidative phosphorylation with the help of a
diagram. 2+5
. Mention the
difference between competitive and non-competitive inhibition with
Lineweaver Burk
plot. 2+5
3. Give an explanatory note on the following
(any four):
3x4=12
a) Active site of an enzyme.
b) Role of blood buffer in the
maintenance of acid base balance.
c) Watson-Crick model of the DNA.
d) Pseudo nucleotide as coenzyme.
e) Fluid mosaic model of biomembrane.
4. Explain the following statements: 3+3+3+3
a) Glucose enhances the absorption of the
Na+ from the intestine.
b) Coenzymes are the co-substrates in the
enzymes.
c) Lecithin is an amphipathic molecule.
d)
Immunoglobulins are classified on the basis of type of heavy chain present in
them.
MODEL
QUESTIONS IN BIOCHEMISTRY
FIRST
PROFESSIONAL M.B.B.S EXAMINATION
BIOCHEMISTRY
(SECOND PAPER) F.M-50
1) Describe only one
of the following:
a) Describe the
glycolytic pathway in erythrocytes. Calculate the total energy
production
when one more of glucose is utilized by them. Indicate the importance
of 2,3 DPG
generated in this pathway. 8+2+2=12
b)
Describe the formation of urea in the body. Mention how ammonia is
disposed off
by other methods. 8+4=12
2) Describe any two of the following:
a) Describe the
chemical composition and indicate the metabolism of very low
density
Lipoprotein (VLDL) with the help of a flow diagram. 2+5=7
b) Write down the chemical structure and
mechanism of action of insulin. 3+4=7
c) Mention the
steps of heme biosynthesis with its control mechanism.
5+2=7
3) Give an explanatory notes on any four of the
following: 3+3+3+3=12
a) Genetic code
b) Recombinant
DNA technology
c) Cyt P450
d) Polymerase
chain reaction.
e) Point
mutation.
4) Explain the following statements:
3+3+3+3=12
a) Glucose can be
converted to fatty acids but the fatty acids cannot be converted to
glucose in
human.
a) Fructose leads
to formation of more VLDL.
a) Metabolism of
glucose is controlled by Phosphofructokinase.
a) Glycogen
storage diseases often leads to hypoglycemia.
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