BIOCHEMISTRY
(INCLUDING MEDICAL PHYSICS AND MOLECULAR BIOLOGY)
I) GOAL
The broad goal of teaching undergraduate students in Biochemistry is to make them
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understand the scientific basis of life processes at the molecular level and to orient themtowards the application of this knowledge in solving clinical problems
II) OBJECTIVES
(A) Knowledge: At the end of the course, the student shall be able to;
(a) Describe the molecular and functional organization of a cell and lists its sub cellular
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components.(b) Delineate structure, function and inter-relationship of bimolecular and consequences of
deviation from normal.
(c) Summarize the basic and clinical aspects of Enzymology with emphasis on diagnostic
enzymes.
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(d) Describe digestion & assimilation of nutrients and consequences of malnutrition(e) Integrate the various aspects of metabolism and their regulatory pathways
(f) Explain the biochemical basis of inherited disorders with their associated consequence
(g) Describe mechanisms involved in maintenance of body fluid, and pH homeostasis
(h) Outline the molecular mechanisms of gene expression and regulations, the principles of
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genetic engineering and their application in medicine.(i) Summarize the molecular concept of defenses and their application in medicine.
(j) Outline the biochemical basis of environmental health hazards, biochemical basis of
cancer and carcinogenesis
(k) Familiarize with the principles of various conventional and specialized laboratory
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investigations, instrumentation analysis and interpretation of a given data.(l) Suggest experiments to support theoretical concepts and clinical diagnosis.
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(B) Skills At the end of the course, the student shall be able to
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1. Make use of conventional techniques and instruments to perform biochemical analysisrelevant to clinical screening and diagnosis
2. Analyze and interpret investigative data
3. Demonstrate the skills of solving scientific and clinical problems and decision making
(C) Integration: The knowledge acquired in Medical Biochemistry shall help the students
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to integrate molecular events with structure and function of the human body in healthand diseases.
DURATION
Duration of the course: 2 semesters
Total number of hours: 240 (Lectures: 160 Hours & Practicals and Innovative sessions:
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80Hrs) Innovative sessions include projects, seminars, structured discussion, integratedteaching, formative evaluation and revision
DETAILED SYLLABUS DETAILS OF COURSE BIOCHEMISTRY:
Essays must be framed from topics with three stars.
Five and three marks questions must be framed from topics with three stars or two
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stars.[THEORY: 160Hrs]
PAPER 1 (90Hrs)
S NO TOPICS
Hrs
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1CELL
(2Hrs)
1.1
**Structure and Functions of cell and cellular organelles
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1Hr** Diseases associated withorganelle.
1.2
Fractionation of organelles (in brief) and their marker enzymes
1Hr
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2BIOMOLECULES
(15Hr
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2.1PROTEINS: ** Classification of aminoacids based on structure, metabolic fate, 1Hr
nutritive value
**Properties of amino acids: Ionic properties of amino acids, Isoelectric pH
2.2
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and its1Hr
importance; Buffering action of aminoacids and proteins
2.3
**Peptide bonds; Biologically important peptides;
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1Hr***Structural organization of proteins Primary Structure of insulin
2.4
**Secondary structure
1 Hr
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2.5**Tertiary and Quaternary structure ; Myoglobin, Collagen and hemoglobin;
1Hr
Protein folding in brief, Prion Diseases
*Proteins: Classification based on composition & solubility, shape, function
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2.6and nutritional value, limiting aminoacids and mutual supplementation
1Hr
**Denaturation, Coagulation; Precipitation of protein ?Isoelectric precipitation
2.7
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,1Hr
precipitation using salts ,heavy metals and organic solvents
2.8
CARBOHYDRATES:**Classification,**Isomerism
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1Hr2.9
*Reactions: Reducing property ,Oxidation, Reduction, Dehydration and
1Hr
Condensation (Details of reactions along with practicals)
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2.10*Glycosidic bonds ? N linked & O linked with examples
1Hr
*Amino sugars, deoxy sugars with examples
*Disaccharides ? reducing & nonreducing , Highlight clinical importance of
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lactulose2.11
**Polysaccharides : Homopolysaccharides , Heteropolysaccharides
1 Hr
**Glycosaminoglycans ? composition, distribution and function
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* mucopolysaccharidosis ? Types ,common features & enzyme deficiency2.12 *Blood group antigens ? Basic composition &Types
1Hr
**Dietary fibre ? Definition, types function & clinical significance
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2.13 LIPIDS: ** Definition, Classificationwith examples
1 Hr
* Fatty acids: Definition, Alpha and omega numbering system, Classification ;
Clinical significance of MUFA & PUFA; Essential fatty acids;Trans fatty acids
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2.14 *Cholesterol : Structure, Biologically important compounds derived1 Hr
*TAG : Composition & Function
**Phospholipids ? Composition & Functions
*Phospholipases- Clinical highlights: Viper venom ,Respiratory distress
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syndrome** Membranes : Structure & Composition (Functions will be dealt in
2.15 Physiology
1Hr
classes)
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*Micelle & Liposomes3
ENZYMES
(7Hrs)
3.1
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**Definition, IUBMB classification with examples, Coenzymes & Cofactors1Hr
**Concept of active site, Specificity of enzymes ;Factors affecting enzyme
3.2
activity ,
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1HrKm value and its significance
3.3
***Enzyme inhibition : Competitive, noncompetitive, uncompetitive with
1 Hr
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examples***Suicidal inhibition, Allosteric inhibition and feedback inhibition with
3.4
examples
1 Hr
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(High light : Enzyme inhibition and drug designing)3.5
*** Enzyme regulation in biological systems ? Compartmentalization,allosteric 1Hr
regulation, covalent modification, zymogen activation, induction , repression &
Derepression
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3.6** Clinical enzymology: Diagnostic importance of enzymes ; Functional &non
1 Hr
functional enzymes;
**Iso-enzymes : Definition, Separation and examples ? CPK & LDH
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3.7**Other enzymes of diagnostic importance: Transaminases( AST,ALT),
1Hr
ALP,GGT,NTP,ACP,Amylase,Lipase,Choline esterase,Enolase
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*Therapeutic enzymes
*Enzymes used in laboratory techniques
4
DIGESTION AND ABSORPTION
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(4)CARBOHYDRATES: **Digestion, Absorption, Glucose transporters (mechanism
4.1
not
1Hr
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needed) (Emphasize the relation of salt in the diet & ORS)** Significance of dietary fibre
*Glycemic index: Definition & Clinical significance
*Malabsorption: Lactose intolerance
4.2
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LIPIDS: ***Digestion ,Role of bile salts & micelle2 Hr
*Absorption of lipids ; *Malabsorption: Steatorrhea
4.3
PROTEINS: *Digestion & Absorption, Meister cycle
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1Hr*Nitrogen balance, PEM, Definition of balanced diet, Limiting amino acids,
4.4
BMR
1Hr
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5METABOLISM OF CARBOHYDRATES
(19)
5.1
***Glycolysis ; Definition,reactions,energetics,rate limiting step,Regulation
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2Hrs5.2
**Rappaport Lubering pathway, Significance of 2,3 BPG, Cori's cycle
5.3
**Fate of pyruvate,PDHreaction,lactic acidosis with two examples
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1Hr5.4
***Gluconeogenesis ; Definition, substrates, reactions & key enzymes,
2 Hrs
5.5
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Regulation, Significance, *,Glucose alanine cycle5.6
**Glycogenesis
3Hrs
5.7
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Glycogenolysis; Regulation in brief5.8
*Glycogen storage disorders ? Von Gierke' s disease in detail
**HMP shunt pathway; Tissues operating , Oxidative phase in detail & mention
5.9
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the2Hrs
products of non oxidative phase,
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5.10 **Significance of HMP shunt pathway,G6PD,Transketolase5.11 **Minor sugars; Galactose metabolism & disorders ; Fructose metabolism &
1Hr
disorders
5.12 *Uronic acid pathway in brief, Significance of the pathway,Pentosuria;Polyol
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1Hrpathway and its importance
***Regulation of blood glucose : Fed & fasting state; Organs, Glucose
5.13 transporters,
1Hr
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Hormones, Enzymes involved5.14 **Insulin : Receptor ,mechanism of action, insulin release , Actions of insulin
1Hr
related to metabolism in brief
***Diabetes Mellitus: Definition ,Types & etiology ,Diagnostic criteria,
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5.15 Metabolic1Hr
derangements
5.16 ***Acute & chronic complications (Biochemical basis)
2Hrs
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5.17 ***Laboratory diagnosis and monitoring of glycemic control and complications5.18 **GTT: Indications, Procedure, Interpretation .Types of GTT curves.
1 Hr
Mini GTT,Extended GTT,IV GTT & GCT in brief
5.19 **Hypoglycemia:Definition,causes,clinical features ,biochemical basis of
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1 HrManagement, Glycosurias and reducing substances
6
METABOLISM OF LIPIDS
(18Hr
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s)6.1
**Fatty acid biosynthesis: Fatty acid Synthase complex, reactions ; Regulation ; 2 Hrs
6.2
*Elongation and desaturation of fatty acids
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6.3Fatty acid oxidation:*** Beta oxidation ; Definition, Fatty acid transport
2 Hrs
6.4
&carnitine,steps.
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27Energetics ,regulation & disorders
6.5
**Oxidation of odd chain fatty acid & fate of propionylcoA
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2Hrs6.6
*Oxidation of unsaturated fatty acid & very long chain fatty acid
*Alpha & Omega oxidation of fatty acid; in brief ; * In born errors associated
6.7
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***Ketone bodies : Formation & utilization1Hr
***Metabolic background of ketoacidosis in DM and starvation and
6.8
differential
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1Hrdiagnosis by laboratory
**Adipose tissue : Types, Liver adipose tissue axis , Adipokines ; Hormone
6.9
sensitive
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1Hrlipase
6.10 **Fatty liver: Causes, Lipotropic factors, fate of fatty liver
1Hr
6.11
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**Cholesterol : Synthesis up to mevalonate in detail and mention the1 Hr
intermediates of important reactions up to cholesterol, Regulation
6.12 **Metabolic fate: Formation of bile salts and its significance , Mention other
1Hr
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biologically compounds derived from cholesterol6.13 **Lipoproteins : Definition, General structure of lipoproteins, classification,
2Hrs
6.14 separation; ***Metabolism of chylomicrons
6.15 ***Metabolism of VLDL & LDL
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1 Hr6.16 ***Metabolism of HDL **Different types of HDL &Lp(a) and their significance 1Hr
6.17 *Lipid profile; Dyslipidemia; Dietary management & role of statins
1Hr
Lipid storage disorders : NiemannPick,Taysach';s,Gaucher's,Fabry'sdisease in
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brief6.18 Eicosanoids : ** Prostaglandins &Thromboxanes ; Major steps of
1Hr
formation;**Biochemical actions & therapeutic uses*Mention
Leukotrienes&Lipoxins
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7METABOLISM OF AMINOACIDS
(20Hr
s)
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*Dynamic state of body proteins, Body aminoacid pool; Inter organ transport
7.1
ofamino acids,* Nitrogen balance and PEM
1 Hr
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**Reactions; Transdeamination ( transamination + Oxidative deamination);7.2
Non oxidative deamination
1Hr
7.3
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***Formation and detoxification of ammonia (urea Cycle)2Hrs
Regulation, Energetics, Hyperammonemia ,Biochemical basis of management
7.4
of hyperammonemia
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7.5**One carbon metabolism
1Hr
7.6
***Metabolism of glycine:, Compounds synthesized and inborn errors
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2 Hrs7.7
**metabolism of serine, role as a component of proteins
1Hrs
7.8
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**Metabolism of Sulfur containing amino acids: Metabolism of Cysteine2Hrs
7.9
Glutathione,Taurine,Transulfuration,PAPS ;*Excretion of Sulfur
7.10 **Metabolism of Methionine,Transmethylation
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2Hrs7.11 Inborn errors associated with metabolism of S containing amino acids
***Metabolism of aromatic amino acids: Phenyl alanine and tyrosine;
7.12 Compounds
3Hrs
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7.13 synthesized, Inborn errors associated**Catabolism of catecholamines ,VMA formation & excretion and its
7.14 significance
7.15 **Metabolism of Tryptophan and compounds (niacin melatonin, serotonin,
2Hrs
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7.16 indoxyl) formed in brief**Hartnup disease and its diagnosis** Effect of PLP on Tryptophan
metabolism
*Formation and excretion of 5HIAA and its clinical significance
7.17 * Histidine metabolism & Inborn error associated**FIGLU excretion test
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1Hr*Glutamic acid ,GABA; Glutamine ; *Aspartic acid ,Asparagine
7.18 *Metabolism of Arginine, NO, Polyamines.
3Hrs
7.19 *Branched chain aminoacid metabolism (1st two steps only required) &MSUD
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*Biologically important amines ; *Amino acids and amino acid derivatives7.20 acting as
neurotransmitters ; *Organic acidurias
8
TRICARBOXYLIC ACID (TCA) CYCLE & ELECTRON TRANSPORT CHAIN (ETC)
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(4Hrs)29
8.1
***TCA Cycle: Final Common oxidativePathway of metabolism
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2 Hrs8.2
Reactions,regulation,energetics& inhibitors; Anaplerotic
reactions;Amphibolic role
8.3
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**High energy compounds: definition and examples2Hrs
8.4
***ETC : Components and sites of ATP synthesis; Mechanism of oxidative
phosphorylation; ATP synthase Inhibitors **Brown adipose tissue
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** integration of metabolism, Adaptations in starvation: Life style diseases, BMI8.5
obesity, Metabolic syndrome(Mention NASH, PCOS) Atherosclerosis
2 Hrs
PAPER 2 (70Hrs)
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9METABOLISM OF HEME
(8
Hrs)
9.1
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***Heme synthesis : Heme synthetic pathway ,regulation &effects of lead2Hrs
9.2
poisoning
**Porphyrias: Types,Enzyme defects,manifestions and investigations of blood
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9.3&
1Hr
urine (Acute intermittent Porpyria in detail and others in brief)
9.4
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***Heme catabolism: Formation & fate of bilirubin (uptake, conjugation,1Hr
secretion) ;Formation & Fate of urobilinogen&stercobilinogen
9.5
***Serum bilirubin: Types, Blood levels in healthy subjects ; Properties;
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2Hrs9.6
***Jaundice: Definition, Classification , Causes &differential diagnosis by
biochemical tests
9.7
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*Neonatal hyperbilirubinemia ,Kernicterus & biochemical basis of treatment in 1Hrbrief
9.8
*Haemoglobinopathies : Different types and Hbs in detail(Hb electrophoresis
1Hr
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,Sickling test)*Thalassemias : Alpha and beta thalassemia in brief10
FAT SOLUBLE VITAMINS
(5Hrs)
10.1 ***Vitamin A : Different chemical forms, dietary sources, RDA Vitamin A;
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2Hrs10.2 Absorption ,transport and storage; Functions of vitamin A ,Wald's visual cycle
Deficiency manifestations and its prevention ; Hyper vitaminosis
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10.3 ***Vitamin D : Chemical nature , dietary sources, RDA Vitamin D;2Hrs
10.4 Active form of vitamin D ? its formation and actions
Deficiency manifestations in children and adults and its prevention
10.5 **Vitamin K: Chemical forms, dietary sources, biochemical Functions ,RDA and 1Hr
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deficiency manifestations Highlight: Vitamin K administration to pretermbabies
&Vitamin K and Prothrombin time
**Vitamin E: Chemical forms, Biochemical Functions (focus lipid peroxidation
and antioxidant function in brief) and deficiency manifestations
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11WATER SOLUBLE VITAMINS
(6Hrs)
**Thiamine: Chemical nature, dietary sources, RDA,coenzyme form,
11.1 biochemical
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1Hrfunctions , deficiency manifestations High light : Transketolase assay to detect
deficiency
*Riboflavin, Pyridoxine: Chemical nature, dietary sources,RDA, coenzyme
11.2 form, biochemical functions , deficiency manifestations
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1Hr11.3 *Pantothenic acid, Niacin, Biotin: Chemical nature, dietary sources, RDA,
1Hr
Coenzyme form, biochemical functions , deficiency manifestations
*Folic acid: Chemical nature, dietary sources, RDA,coenzyme form,
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11.4 biochemical1Hr
functions , deficiency manifestations (One carbon metabolism along with
amino acid metabolism)
**Vitamin B12, Vitamin C: Chemical nature, dietary sources, RDA, role as
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11.5 coenzymes2Hrs
11.6 Biochemical functions, deficiency manifestations ; *Antivitamins
12
MINERALS
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(6Hrs)12.1 *Classification of minerals based on RDA
2Hrs
**Calcium: Dietary sources, biochemical functions, RDA, Blood levels in
12.2 healthy
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subjects, regulation of blood calcium level, Hypocalcaemia, Hypocalcaemia.Phosphorus, Magnesium, Copper: Dietary sources, biochemical functions
12.3 ,RDA,
1Hr
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Disorders related.
12.4 ***Iron: Dietary sources, RDA,; Absorption ,transport &storage; Causes of iron 2Hrs
12.5 deficiency & Iron deficiency Anemia ; Hereditary Hemochromatosis.
*Iodine,Potassium,Sodium,Chloride,Zinc,Selenium,Fluoride,Manganese,Magne
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12.6 siu m : in brief1Hr
13
HOMEOSTATIC MECHANISMS IN THE BODY
(5Hrs)
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Acid base balance: *Acids, bases, pH, pK, Buffers,HendersonHasselbalch13.1 equation
2hrs
13.2 ***Body buffers , respiratory & renal regulation of blood pH
13.3 **Disorders of acid base balance ;
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2Hrs13.5
*Anion gap Assessment of acid base balance by blood gas parameters
13.6 Fluid and electrolyte balance:
1Hr
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*Regulation of osmolality and maintenance of fluids in the various bodycompartments and related disorders
14
MOLECULAR BIOLOGY
(22Hr
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s)14.1 *Nucleotide chemistry : Structure of purine &pyrimidine bases, nucleosides,
1Hr
nucleotides
14.2 Purine synthesis and catabolism:
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1 Hr*Purine synthesis: Synthetic pathway in brief ? Source of constituent atoms
,rate
limiting steps ,first nucleotide formed and the formation of other nucleotides
from
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IMP14.3 ***Purine catabolism: Pathway ,Hyperuricemia,Gout,Biochemical principles of 1 Hr
treatment of Gout ; *LeschNyhansyndrome,Hypouricemia
14.4 *Pyrimidine synthesis and degradation,Oroticaciduria
2Hrs
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14.5 *Synthesis of dNTPs (deoxy nucleotide triphosphates)*Nucleotide analogues & Folic acid antagonists
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14.6 **Nucleic acids: Structure and organization of DNA; Different types of DNA,
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2Hrs14.7 Different types of RNA ,difference between DNA & RNA ;*Mitochondrial DNA
14.8 *Cell cycle and ***Replication: Process of replication (prokaryotes); DNA
2Hrs
14.9 polymerase(prokaryotes & eukaryotes); Inhibitors
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14.10 **DNA repair mechanisms, Examples of DNA repair defects,*Telomerase1Hr
***Transcription: Process of transcription(prokaryotes and differences in
14.11 eukaryotes); RNA
2Hr
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polymerases(prokaryotes & eukaryotes); Inhibitors14.12 **Post transcriptional modifications (hnRNA& primary tRNA transcript)
1Hr
*RNA editing with an example (apo B48&apo B100);*Reverse transcriptase ; *
Ribozyme
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14.13 **Genetic code , **t RNA ; *Ribosomes &Polysomes1Hr
***Translation: Different phases of translation(eukaryotes differences in
14.14 prokaryotes);**Post translational
2Hrs
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14.15 modifications; Inhibitors protein targeting14.16 *Regulation of gene expression (lac operon model, gene amplification, gene
2Hrs
14.17 rearrangement)
DNA based techniques: **Recombinant DNA technology Applications in
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14.18 clinical medicine1Hr
14.19 **Applications in clinical medicine; Gene therapy ,RFLP ,DNA finger printing
1Hr
14.20 **Blotting techniques (Southern, Northern & Western) ; ** PCR*Antisense
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1Hrtherapy
*Biochemical basis of inherited disorders & screening of genetic disorders;
14.21 Mode of inheritance
1Hr
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14.22 ***Mutations: Definition ,types with examples ; Mutagens ,Ame's test1Hr
15
IMMUNOGLOBULINS
(3hrs)
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**Immunoglobulin: Types, Structure (general structure and structure of IgM&15.1 IgA);
2Hrs
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15.2&Functions ; *Hypergammaglobulinemia ; * Hypergammaglobulinemia
15.3 *AIDS (Structure of HIV virus ,major genes & antigens), Natural course of HIV
1Hr
infection Immunology of AIDS, Laboratory diagnosis &monitoring, Biochemical
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basis of retroviral therapy16
BIOCHEMISTRY OF CANCER
(3Hrs)
16.1 **Biochemistry of cancer: Cell cycle, Cyclins and apoptosis. Etiology of cancer; 2Hrs
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16.2 Carcinogensesis: Oncogenic virus; Oncogenes ;Tumor suppressor genes,16.3 **Tumor markers ; *Anticancer drugs * Monoclonal antibodies
1Hr
17
CLINICAL BIOCHEMISTRY
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(7Hrs)**Plasma proteins: Types ; Functions ; Separation ; Abnormal patterns in
17.1 clinical
1Hr
diseases ; A G ratio; Acute phase proteins
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**Electrophoresis of serum proteins ;Multiple myeloma &Bence Jones17.2 proteins
1Hr
**Chromatography and diagnosis of inherited disorders of metabolism
(Example: Aminoaciduria)
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17.3 *Colorimetry *ELISA (Principle, Procedure ,Applications),*Radio immune assay 1Hr(RIA)
17.4 ** Cardiac markers ***Liver function tests and interpretation
1Hr
17.5 *Thyroid function tests and interpretation
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1Hr17.6 **Renal function tests and interpretation
1Hr
*Radioactivity :Radioactive isotopes used in Medicine ;Diagnostic, therapeutic
17.7 and
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1Hrresearch applications; Radiation hazards
18
XENOBIOTICS
(2Hrs)
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18.1 **Detoxification and Biotransformation of xenobiotics: Different phases2Hrs
18.2 *Metabolism of alcohol, brief mention of environmental toxins
19
FREE RADICALS AND ANTIOXIDANTS
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(1Hr)Free radicals: Generation, Types, lipid peroxidation. Antioxidants: Different
19.1 types
34
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PRACTICAL SYLLABUS [TOTAL: 80Hrs]
QUALITATIVE EXPERIMENTS
Topics
2 Hr
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SessionsReactions of Carbohydrates : Glucose ,Fructose,Lactose,Sucrose
4 (8hrs)
Proteins : Precipitation of Proteins
1 (2Hrs)
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Proteins: Color reactions1(2Hrs)
Reactions of Albumin
1(2Hrs)
Reactions of Urea,Uric acid &Creatinine
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1(2Hrs)Identification of biologically important substance in given solution
1(2Hrs)
Normal constituents of urine ? Inorganic & Organic constituents
2(4Hrs)
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Abnormal constituents of urine2(4Hrs)
Demonstration of electrophoresis of serum proteins & interpretation
1(2Hrs)
Demonstration of paper chromatography/TLC urinary aminoacids& interpretation
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1(2Hrs)Hemin crystal preparation and microscopic examination
1(2Hrs)
QUANTIATIVE EXPERIMENTS
Introduction to clinical chemistry: Collection of blood samples, Anticoagulants ,
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Collection of 24 hour urine sample and Urine preservatives1(2Hrs)
Principles of colorimetry
Estimations of levels of glucose, urea, creatinine, total protein and albumin in blood 5(10Hrs)
CHART DISCUSSION Clinical cases along with biochemical test results for
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interpretation and discussionJaundice ? Hepatic ,Hemolytic and Obstructive jaundice
1(2Hrs)
Diabetes mellitus -
Cases based on diabetes mellitus, Diabetic ketoacidosis, Hyper 1(2Hrs)
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35osmolar nonketotic coma, Hypoglycemia ,IGT,IFG
GTT curves ? Normoglycemia, Diabetes mellitus, IFG, IGT, Alimentary glycosuria,
Renal glycosuria ,Hypoglycemia
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1(2Hrs)Charts based on HbA1C &Micro albuminuria
Myocardial infarction : Markers
1(2Hrs)
Pancreatitis : Markers
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Prostate Cancer : MarkersNephrotic syndrome,
Glomerulonephritis
Charts based on alcoholism, atherosclerosis, lipid profile, fatty liver
1(2Hrs)
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Charts based on acid base parametersrelated to Metabolic acidosis, Metabolic
alkalosis, Respiratory acidosis and Respiratory alkalosis (Only uncompensated cases)
Charts based on TFT related to Hypothyroidism & Hyperthyroidism
1(2Hrs)
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Charts based on Metabolic syndrome ,GoutCharts based on inborn errors of metabolism (Lactose intolerance ,
Galactosemia, Fructosuria, vonGierke's disease, PKU, MSUD,
Hartnup's
disease,
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Alkaptonuria ,Albinism, Pheochromcytoma Carcinoid syndrome, Lesch Nyhansyndrome
Charts based on Vitamins: Vit A ,D ,K, Thiamine,Niacin,Ascorbicacid,Pyridoxine,Folic 1(2Hrs)
acid
Charts based on Minerals:
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Hypocalcaemia, Hyperkalemia, Hypokalemia,Hyponatremia,
Hyponatremia,
Fluorosis
,Iron
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deficiencyanaemia, Haemochromatosis, Wilson's disease
Charts on replication fork, Xeroderma pigmentosum , HNPCC , HIV major genes &
antigens
1(2Hrs)
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36Charts based on enzyme inhibition: Competitive Non competitive, Suicidal
inhibition
OBJECTIVE STRUCTURED PRACTICAL EXAMINATION (OSPE)Practice sessions
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2 (4Hrs)SPOTTERS: Based on tests, instruments, charts, microscopic slides, graphs,
nutrition,
1 (2Hrs)
reference ranges of routine parameters, major concepts, reagents, Indicators.
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Seminars :7
(Guide lines for evaluation.( Colleges can
make their own marking scheme)
(12Hrs)
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Allot 10 topics for a day.Assign a single topic for a student for presentation lasting for 10 minutes
All the students should learn all the 10 topics. Those who present topic will
be evaluated based on the presentation; others will be evaluated either by
MCQ based post test or assignments based on the topic presented.
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(10 MCQs just after the presentation part of the session or assignmentsubmitted within a week)
Marks: 10 marks for presentation & 10 marks for MCQ
Consider 10 % of this mark for internal assessment
Distribution of marks for practical session
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ItemsMarks
Qualitative experiment
10 marks.
The questions may be reworded so
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that the application of theexperiment is highlighted.
Question cards may be used
to elicit more information
Sample questions are provided below
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which are only for guidance. Colleges canprepare their own question bank.
10 marks The questions may be reworded
so that the application of the experiment is
highlighted
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Quantitative experimentSample questions are provided below
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which are only for guidance. Colleges can
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prepare their own question bankChart discussion
10marks
Spotters
5 marks -10 spotters ? 10x0.5=5 marks
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5 marks. Two OSPE stations with 2.5marks each. One performance station
and one writing station using suitable
question cards.
Sample questions and grading sheets provided
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OSPEfor guidance only
Record
[Assessment of record keeping should be
done along with internal assessment. But
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submission of record during UniversityPractical Examination is compulsory ,
to
meet the requirement of attending practical
examination]
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Sample questions for QUALITATIVE EXPERIMENTI. i) Identify whether the sugar solution contains a monosaccharide or disaccharide?
[By doing relevant tests (Benedict's test, Barfoed's test/ Alkali destruction test , it is to be
identified and reported).
ii) Related questions (2 or 3 questions may be kept on the seat as a question card) some
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examples related to the above question are given below1. Name 2 reducing disaccharides. What are their components?
2. What is the type of linkage between the monosaccharides in these sugars?
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3. What is the shape of the osazone?4. Name a condition where a disaccharide is excreted in urine
5. Name the dietary source for any of these disaccharides
6. Which enzyme can hydrolyze it in the GIT?
7. What will happen if this enzyme is deficient?
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Q II.i) Observe the results of these tests and suggest the identity of the sugar. Do you needany other test to confirm the nature of the sugar? If so perform the test and confirm
Q III.i) How will you identify the monosaccharide supplied in the solution? Glucose or
fructose
Some questions related to the above question are given below Q II &Q III
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1. Give 2 differences between these sugars2. Name the dietary source
3.Name a disaccharide containing this sugar
4. Name a homopolysaccharide containing this sugar
Q IV.With the help of a test explain the reducing property of glucose
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1. What is the clinical use of this test?2.Is this test specific for glucose?, if not name two non carbohydrate and two carbohydrate
substances giving this test positive?
3. Name a test that specifically detects glucose.
Q V. The urine sample from a 6 year old boy gave a positive Benedict's test. Mother
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complains that the child is losing weight in spite of increased appetiteIdentify the sugar (performance of tests)
1. Enumerate the causes of Glycosurias
2. Give two inherited causes of Glycosurias
3. Name a non sugar reducing compound
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4. Is there an indication for performing plasma glucose estimation in this patient? If so explain.39
Sample questions for QUANTITATIVE EXPERIMENT
Q I. A retired school teacher aged 62 yrs complaining of increased thirst, hunger, passing
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urine more frequently and losing weight. Urine showed glucose oxidase based strip testpositive.
1. What is the blood test required to diagnose diabetes mellitus and Do it & furnish the result.
[The examiner can discuss the value obtained, method used and possible causes of an
abnormal result at the end. ]
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2. Give the diagnostic criteria of diabetes mellitus3. What are IFG and IGT?
4. Name a blood test that reveals mean glucose level over the previous 12 weeks. What is
the level of this parameter suggestive of normal glycemic status?
5. Name one test used as a early marker of diabetic nephropathy and retinopathy
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Q II. A 5 year old admitted to pediatric ward due to severe diarrhea vomiting and reducedurine output. He is dehydrated. A sample of blood is sent for investigations to assess the
renal function.
1.Name two blood test useful to assess renal function
2. Name the analyte which is elevated in dehydration and also in renal disease. Do
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the estimation of it and submit the report.3.What is the current Gold standard test to detect renal function
OSPE General Guidelines:
OSPE questions prepared for experiments should be observable and structured and
should be completed within five minutes.
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In addition to experiment, the questions kept at the writing station willhelp to derive the concealed concepts related to the experiment eg: inference /clinical
correlations/reference range etc.
A few model OSPE questions are furnished below along with check list for structuredobservations.
A set of common laboratory reagents and lab ware should be arranged at the station. Sothat students
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can select the required reagents according to the OSPE questions.Advantages OSPE:
practising OSPE questions will sharpen the skills
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Sample OSPE questions1. Glucose solution is provided in a numbered beaker/test tube. Show that it is an aldose
by doing one test
Steps
Observations
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MarksSelection of a test to show glucose is an aldose : Seliwanoff's test/
1
Rapid Furfural test
0.5
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2Step-1
0.5
3
Step-2
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0.54
Write down the observation and inference
0.5
Overall performance of the student in terms of choice of proper glassware,
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5Cleanliness , handling of reagent bottles ,accuracy and precision.
0.5
2. Demonstrate the amino acid Tyrosine/Tryptophane, in the given protein solution.
3. Test to distinguish monosachharides from disacharides
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4. Test to demonstrate the presence of ketone bodies / bile salts in urine5. Test to detect the presence of uric acid/creatinine in a solution
Note: Appropriate question cards with a minimum of 3 questions, may be used at the writing station.
MARKS
University examination
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MarksTheory paper I & II ( 50+50)
100
Theory - Internal assessment
20
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Viva20
Practical
40
Practical - Internal assessment
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20Total
200
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SUGGESTED BOOKS IN BIOCHEMISTRYBooks for study:
1. Text of Biochemistry for Medical students by Vasudevan & Sreekumari
2. Harper's review of Biochemistry- latest edition
3. Text of Biochemistry for Medical students R Text of Biochemistry for
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Medical students Rafi M.D4. Lippincott's Il ustrated Review of Biochemistry -latest edition
5. Practical Biochemistry for Medical students by Vasudevan
6. Practical Biochemistry by Geetha Damodaran K
7. Manual of Practical Biochemistry by S K Gupta,Veena Singh Chalaut&Anju Jain
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Books for Reference:1. Principles of Biochemistry by Lehninger
2. Biochemistry with Clinical Correlations by Thomas. M. Devlin
3. Biochemistry by Stryer
4. Biochemistry-A case oriented Approach by Montgomery
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