PERIYAR UNIVERSITY

Periyarpalkalai Nagar, Salem-636011

(Reaccredited with ‘A’ grade by the NAAC

DEPARTMENT OF BIOCHEMISTRY

M.Sc. DEGREE
[Choice based credit system(CBCS)]

OBE REGULATIONS AND SYLLABUS

(Effective from the academic year 2018-2019 and thereafter)

1. Preamble

The Department of Biochemistry was established in the year 2005. The department
comprises of two Assistant Professors and two Associate Professors. The main objective of
the department is to inculcate the basic concepts and applications of Biochemistry and thrive
in the field of research and development. The department is known for its commitment to the
self development of students into well-molded individuals who can take on leadership role in
Industry, Academic or Government organization. The Department aims in developing
human resources in Biochemistry and to expand and transfer knowledge in particular
to the rural community residing in and around Salem district of Tamil Nadu, India.
There is a greater demand globally, for trained manpower in the areas of
Biochemistry for Research and Development in multinational companies, public
sectors, quality control labs, biopharmaceutical companies, food industries as well
as in universities. The Department is inbuilt and established with numerous research
facilities such as high speed ultra centrifuges, spectrophotometers, semi autoanalyser,
colorimeter, deep freezers, Cold room, sonicator, Gel documentation system, orbital shakers,
PCR machines, CO2 incubators, ELISA Reader, centrifuges, incubators, laminar flow,
electronic balance, etc.

2. General Graduate Attributes

The graduate attributes reflect both disciplinary knowledge and understanding, skills,
competencies, that students should acquire/attain and demonstrate while studying
Biochemistry program. Some of the characteristic attributes that a graduate should
demonstrate are as follows:

1. Disciplinary knowledge: Capable of demonstrating comprehensive knowledge and

understanding of Biochemistry
2. Communication Skills: express thoughts and ideas effectively in writing and orally
3. Critical thinking: Capability of analyzing, interpreting, discussion by following
scientific approach to knowledge enrichment.
4. Problem solving: apply one’s learning to real life situations.
5. Analytical reasoning: ability to analyze and solve problems quickly and effectively
6. Research-related skills: Ability to define problems, analyse, interpret and draw
conclusions from data and report the results of an experiment or investigation.
7. Cooperation/Team work: Ability to work effectively as a member of a team rather
than individually.
 8. Scientific reasoning: Ability to evaluate ideas and evidence of a particular problem
and reason them based on scientific approach.
9. Reflective thinking: ability to learn from experience
10. Information/digital literacy: Capability to use ICT in a variety of learning
situations.
11. Self-directed learning: Ability to work independently with efficiency based on the
knowledge acquired while learning.
12. Moral and ethical awareness/reasoning: Ability to follow moral/ethical values in
all aspects of work.
13. Leadership readiness/qualities: Capability to guide people to the right destination,
in a smooth and efficient way.
14. Lifelong learning: Ability to acquire knowledge and skills through self-directed
learning aimed at personal development

3. Program specific qualification Attributes

The cognitive domain involves knowledge and the development of intellectual

skills (Bloom, 1956). This includes concepts that serve in the development of
intellectual abilities and skills. There are six major categories of cognitive
processes, starting from the simplest to the most complex

 Knowledge and understanding level (K1 and K2)

 Application level (K3)
 Analytical level (K4)
 Evaluation capability level (K5)
 Scientific or synthesis level (K6)

4. Vision

To achieve academic excellence in Biochemistry by imparting in-depth knowledge to the

students and producing quality students trained in the various facets of Biochemistry,
facilitating research activities and cater to the academic, industrial & societal demands. To
make university a centre of excellence in the discipline of Biochemistry.
5. Program objectives and outcomes

5.1. PROGRAMME EDUCATIONAL OBJECTIVES (PEOs)

The career perspectives of the Master’s program in Biochemistry are

PEO 1: To prepare students for the future careers in the concerned/various relevant fields in
which a core understanding of the chemistry of life is important.

PEO 2: To enable the graduates to exhibit leadership, make life long learners with
professional and social ethics and make them communicate effectively.

PEO 3: To add highly skilled scientific workforce in the area of biomedical research sectors,
academic, industry as well as for research laboratories across the country and the
globe by following best practices for improving the professionalization and
employability of students.

PEO 4: The practical and technical skills with laboratory-based work and the final year
research project prepare the students for a research or technical position by defining
specific and transferable skills.

PEO 5: To sensitize and train the students towards research with typical employers include
pharmaceutical, biotechnology, food, water and agricultural companies and
specialist services, such as toxicological studies.

PEO 6: To train the students in generic and competency skills so as to be able to work in
potential places including scientific and medical publishers and the Intellectual
Property Office

5.2. PROGRAMME SPECIFIC OBJECTIVES (PSOs)

The Overall objective of the Program is to promote education and research in biochemistry
and provide academic and professional excellence for immediate productivity in industrial, or
clinical settings for an ultimate benefit of society and environment.

PSO1: To acquire necessary knowledge and skills in core themes, principles and components of
basic Biochemistry
PSO2: To demonstrate the knowledge of biochemical processes from the cellular and molecular
aspects
PSO3: To Integrate and apply the techniques studied and to compare and contrast the depth of
scientific knowledge in the broad range of fields
PSO4: to be able to understand, analyze and apply the studied basic and concepts in wide
variety of applications including diagnostics, biochemical pathway regulation and drug
development and use this knowledge and apply the same for multitude of laboratory
applications.
PSO5: To provide students with the knowledge and skill base that would enable them to go for
self-employment and entrepreneurship
5.3. PROGRAMME OBJECTIVES (POs)

PO1: To demonstrate comprehensive knowledge on various areas of Biochemistry.

PO2: To acquire skills in areas related to the current and emerging developments.
PO3: To communicate the concepts, constructs and techniques of the subject learnt in a clear,
concise and lucid manner.

PO4: To plan and execute the experiments to the relevant theories of Biochemistry.
PO5: To apply critical thinking, scientific reasoning and mathematical skills in studied areas
of Biochemistry.
PO6: To train the students to acquire various relevant generic and competency skills in
various aspects of biochemistry so as to be able to work independently in a group or
individually

PO7: To make a student life long learner with moral and ethical values

5.4. PROGRAMME OUTCOME (PO’S):-

M.Sc programme in Biochemistry will provide students with the necessary knowledge and
skills to undertake a career in research, either in industry or in an academic setting. The
training provided will give students the breadth and depth of scientific knowledge in
Biochemistry. On completion of the programme, students will be qualified to apply for a PhD
or to gain employment in the pharmaceutical or biotechnology industries, which are among
the strongest growth sectors. The programme will be based on a combination of taught
modules, independent learning and an extended research project to be carried out either in the
University departments or industry or in association with industry at the University. The
programme incorporates a substantial element of hands-on research experience, with
enhanced experimental skills being gained alongside experienced research workers.

It is intended that, on successful completion of the M.Sc degree programme, students will :

1. be capable of demonstrating comprehensive knowledge and have a

fundamental/systematic or coherent understanding of major concepts,
theoretical principles and experimental findings in biochemistry.
2. acquire skills in areas related to the current and emerging developments in the
field of Biochemistry.
3. be identifying and applying appropriate biochemical principles and
methodologies to solve a wide range of problems associated with Biochemistry.
4. communicate the results of studies undertaken in Biochemistry accurately in a
range of different contexts using the main concepts, constructs and techniques of the
subject learnt in a clear and concise manner in writing and oral skills.
 5. Plan and execute the experiments, investigate, analyze and interpret data collected
using appropriate experimental methods, and report the findings of the experiment
and relate the interpretations and conclusions to relevant theories of Biochemistry.
6. They will have the ability to employ critical thinking, scientific reasoning and
efficient problem solving skills in the basic areas of biochemistry.
7. Be able to demonstrate relevant generic skills and competencies such as (i)
problem solving skills, (ii) investigative skills, (iii) communication skills (iv)
analytical skills, (v) ICT skills, (vi) skills such as the ability to work both
independently and in a group.
8. demonstrate professional behaviour such as (i) unbiased and truthful in all aspects
of work (ii) follow moral and ethical practices (iii) Life long learners aimed at
personal development and for improving knowledge/skill development (iv) focusing
on issues related to social cause.

6. Candidate eligibility for admission

Graduates in Biochemistry, Chemistry, Pharmacy, Bachelors of medical lab

technology, Microbiology and Life Sciences as principle subject or Biochemistr y
as subsidiary subject are eligible for admission to the course.

7. Duration of the course: Two year degree programme

8. CBCS structure comprises of two parts

Course Number of Hours of Marks Credits
component courses learning
PART A (Credit courses)
Core courses 11 4 1100 44
Practicals 4 4 400 16
Elective courses 3 4 300 12
Supportive 2 3 200 06
courses
Human rights 1 2 100 02
Research 1 12 100 12
Project and viva-
voce
TOTAL 21 2200 92
PART B (Self learning Credit courses)
Online courses 2 4 200 08
Swayam Course

TOTAL 2 200 08
9. Curriculum structure for each semester
Semes Hrs/w Exam Credits
ter Paper Code Title of the Paper eek Duration

18BCHC01 Core I – Biomolecules 5 3 4

18BCHC02 Core II - Analytical Techniques 5 3 4
18BCHC03 Core III - Advanced Enzymology 5 3 4
18BCHC04 Core IV - Cell Biology and Physiology 5 3 4
I 18BCHE01 Elective I 5 3 4
18BCHP01 Core Practical I (Biochemical Techniques 5 6 4
and Enzymology)
18BCHC05 Core V - Intermediary Metabolism 5 3 4
18BCHC06 Core VI - Plant Biochemistry 5 3 4
18BCHC07 Core VII - Molecular Biology 5 3 4
18BCHP02 Core Practical II (Molecular and Microbial 5 6 4
II Techniques)
18BCHE02 Elective II 5 3 4
18BCHS01 Supportive I 3 3 3
18PHR01 Human Rights 2 3
Internship (4 weeks)
18BCHC08 Core VIII - Genetic Engineering 5 3 4
18BCHC09 Core IX - Advanced Clinical Biochemistry 5 3 4
18BCHC10 Core X – Immunology 5 3 4
18BCHE03 Elective III 5 3 4
III 18BCHP03 Core Practical III (Clinical Biochemistry 5 6 4
and Genetic Engineering)
18BCHS02 Supportive II 3 3 3
Library Hour 2
18BCHC11 Core XI - Drug Biochemistry and Clinical 5 3 4
IV Toxicology
18BCHP04 Core Practical IV (Clinical Biochemistry 5 6 4
and Immunology)
18BCHPR01 Project and Viva-voce 20 - 12
TOTAL 90

Semester Swayam Course Marks Credit

I MOOC-I 100 4
III MOOC-2 100 4

ELECTIVE COURSES
18BCHE 01 - Molecular Endocrinology
18BCHE 02 - Cancer Biology
18BCHE 03 - Biostatistics
18BCHE 04 - Microbiology
18BCHE 05 - Nutritional Biochemistry
18BCHE 06 - Biotechnology
SUPPORTIVE COURSES FOR OTHER DEPARTMENTS
18BCHS 01 - Tools and Techniques in Bioscience
18BCHS 02 - Medical Lab Technology
18BCHS 03 - Clinical diagnosis in health and diseases
18BCHS 04 - Introduction to Biochemistry

10. Credit calculation

Method of teaching Hours Credits

Lecture 1 1
Tutorial/demonstration 1 1
Practical/Internship/ 2 1
Self-Learning

11. CBCS – scheme of examinations semester wise structure

Se Hrs Marks Exam Cre
me Paper Code Title of the Paper /we Durati dits
CIA EA Total
ster ek on
18BCHC01 Core I – Biomolecules 5 25 75 100 3 4
18BCHC02 Core II - Analytical Techniques 5 25 75 100 3 4
18BCHC03 Core III - Advanced Enzymology 5 25 75 100 3 4
18BCHC04 Core IV - Cell Biology and 5 25 75 100 3 4
I Physiology
18BCHE01 Electi ve I 5 25 75 100 3 4
18BCHP01 Core Practical I (Biochemical 5 40 60 100 6 4
Techniques and Enzymology)
18BCHC05 Core V - Intermediary Metabolism 5 25 75 100 3 4
18BCHC06 Core VI - Plant Biochemistry 5 25 75 100 3 4
18BCHC07 Core VII - Molecular Biology 5 25 75 100 3 4
18BCHP02 Core Practical II (Molecular and 5 40 60 100 6 4
II Microbial Techniques)
18BCHE02 Elective II 5 25 75 100 3 4
18BCHS01 Supportive I 3 25 75 100 3 3
18PHR01 Human Rights 2 25 75 100 3
Internship (4 weeks)
18BCHC08 Core VIII - Genetic Engineering 5 25 75 100 3 4
18BCHC09 Core IX - Advanced Clinical 5 25 75 100 3 4
Biochemistry
18BCHC10 Core X – Immunology 5 25 75 100 3 4
III 18BCHE03 Elective III 5 40 60 100 3 4
18BCHP03 Core Practical III (Clinical 5 25 75 100 6 4
Biochemistry and Genetic
Engineering)
18BCHS02 Supportive II 3 25 75 100 3 3
Library Hour 2
18BCHC11 Core XI - Drug Biochemistry and 5 25 75 100 3 4
IV Clinical Toxicology
18BCHP04 Core Practical IV (Clinical 5 40 60 100 6 4
Biochemistry and Immunology)
18BCHPR01 Project and Viva-voce 20 40 60 100 - 12
TOTAL 2200 90
 Semester Swayam Course Marks Credit
I MOOC-I 100 4
III MOOC-2 100 4

Teaching methodologies
The classroom teaching would be through conventional lectures and use of
OHP and Power point presentations. The lecture would be such that the students
should participate actively in the discussion, students seminars would be conducted
and scientific discussions would be arranged to improve their communicative skill.

In the laboratory, instructions will be given for the experiments followed by

demonstration and finally the students have to do the experiments individually.
Periodic tests will be conducted for the students. Slow learners will be given special
attention

12. Examinations
There shall be four semester examinations. Two in the first year and two in
the second year. Candidates failing in any subject will be permitted to appear for
such failed subjects at subsequent examination. The syllabus has been divided into
4 semesters. The examination for the Semester I & III will be held in
November/December and that for the Semester II and IV will be in the month of
April/May. The Practical examination will be conducted at the end of each
semesters. Candidates failing in any of the practical examination will be permitted
to appear for such failed practical examination at subsequent practical examination.

13. Scheme for evaluation and Attainment Rubrics

Theory External : 75 Marks
Internal : 25 Marks

Three test : 10 Marks

Seminar : 5 Marks
Assignment : 5 Marks
Attendance : 5 Marks
 Practical External : 60 Marks
Internal : 40 Marks

Practical test: 30 Marks

Record : 5 Marks
Attendance : 5 Marks

SCHEME FOR PRACTICAL EXAM

Time – 6 hours Max. Marks = 60

I Major
Experiment - I 25
Experiment - II 25
II Viva 5
III Record 5

Procedure 5
Table 4
Graph 4
Calculation 6
Result 6

QUESTION PAPER PATTERN (THEORY)

Part A : Answer All questions (MCQ) 20 x 1 = 20 marks

Part B : Answer any three questions (Analytical reasoning) 3 x 5 = 15 marks
Part C : Answer All questions (either or type) 5 x 8 = 40 marks

Duration of the examination - 3 hours Maximum marks – 75

FOR RESEARCH

S.No. Particulars Marks Examiners

1 Dissertation 30% Internal Examiner
30% External Examiner
2 Viva-voce 20% Internal Examiner
20% External examiner
14. Grading system

Evaluation of performance of students is based on ten-point scale grading system as given

below

Ten Point Scale

Grade of Marks Grade Points Letter Grade Description
90-100 9.0-10.0 O Outstanding
80-89 8.0-8.9 D+ Excellent
75-79 7.5-7.9 D Distinction
70-74 7.0-7.4 A+ Very Good
60-69 6.0-6.9 A Good
50-59 5.0-5.9 B Average
00-49 0.0 U Re-appear
ABSENT 0.0 AAA Absent
 BIOMOLECULES
COURSE CODE : 18BCHC01 L T P C
Hours
3 1 0 4

MARKS : 100
COURSE
OBJECTIVES : To understand the basis of biomolecules which will enable to
demonstrate foundational knowledge about important biomolecules
in cells and living organism, essential to life processes.

COURSE OUTCOMES (CO)

After completion of the course, the students will be able to,

CO1 Understand and demonstrate how the structure of carbohydrates determines their
chemical properties and reactivity. Various functional groups involved in bond
formation / linkage and also encourages the student to draw and recognize key
structures of carbohydrates.
CO2 Understand the structure, functional groups, draw and recognize key structures of
amino acids and function of amino acids, their interactions, various structural aspects
of proteins involved in biology.
CO3 Understand the structure and function of important biological macro molecules like
lipids, its types , composition, its role in biological function. Various functional
groups bond formation / linkage.
CO4 Have knowledge of the structure/conformational freedom of DNA/RNA various
functional groups in bond formation / linkage, functional difference help students to
draw and recognize key structures of nucleic acids, know their functions in biology.
CO5 Know about the structure, types of minerals and vitamins in biological reactions,
and its relationship with disease.

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I Carbohydrate Classification of Carbohydrate - structure, K1,K2,K3 12
s occurrence, properties and biological functions.
Homoglycans - structure and biological
functions. Heteroglycans and complex
carbohydrates : Structure, and biological function.
Mucopolysaccharides – bacterial cell wall
polysaccharides and sialic acid. Lectins –
characteristics and uses, Blood group antigens,
Major classes of glycoproteins: O-linked and N-
linked oligosaccharides.
II Proteins Amino acid 1 and 3 letter abbreviation, K1,K2,K3 14
classification, biologically important peptides.
 peptide bond, peptides. Physical interactions that
determine the properties of proteins – shot range
repulsions, electrostatic forces, van der waals
interaction, hydrogen bond and hydrophobic
interactions. Primary structure and its
determination. The Ramachandran plot and cross
links. Secondary structure :The α-helix, β-sheets
and Corey model for fibrous proteins, super
secondary structures - Zinc motifs, Leucine zipper
motif. Tertiary structure - Collagen and quaternary
structure - Hemoglobin .
III Lipids Classification of lipids. Saturated and unsaturated K1, K2, 12
fatty acids. Derived lipids: Phospholipids, K3
glycolipids, structure and function. Eicosanoids-
structure and biological actions of prostaglandins,
prosracyclins, thromboxanes, leukotrienes and
lipoxins. Lipoproteins- Classification and
composition. Amphipathic lipids – membranes,
micelles, emulsions and liposomes.

IV Nucleic Acids Structure of nucleic acids, Structure of dsDNA – K1, K2, 14

Watson and Crick model of DNA, properties of K3
dsDNA, DNA sequencing procedures- Maxam
Gilbert method and Sanger’s dideoxy methods.
Properties of DNA – denaturation, renaturation,
Cot curves, Crucifrom DNA, Triple stranded
DNA. Triplex and duplex RNA , Major and
Minor classes of RNA- mRNA, t RNA, rRNA, hn
RNA.
V Vitamins and Water soluble vitamins - thiamine, riboflavin, K3, K4 13
Porphyrins niacin, pyridoxine, folic acid, ascorbic acid
sources, structure, biochemical functions,
deficiency diseases, daily requirements.
Fat soluble - vitamin A, vitamin D2, vitamin E and
vitamin K - sources, structure, biochemical
functions, deficiency diseases, daily requirements
and hypervitaminosis. Porphyrins the porphyrin
ring system.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
Text Books

1. Nelson,D.L. and Cox,M.M. 2013. Lehninger Principles of Biochemistry, 6 th

Edition, W.H. Freeman & Co.
2. Berg,J.M. et al., 2012. Biochemistry, 7 th Edition, W. H. Freeman & Co.
3. Voet,D. et al., 2012. Fundamentals of Biochemistry: Life at the Molecular level,
4 th Edition, John Wiley and Sons.

Reference Books
1. Zubay,G.L. 1998. Biochemistry, Wm.C. Brown Publishers.
2. Sinden,S.R. DNA structure and function, First Edition, Academic Press, 1994.
3. Carl Branden and John Tooze, Introduction to Protein Structure, Second Edition,
Garland Publishing, 1999.
4. Garrett,R. and Grisham,C. 2010. Biochemistry, 4 t h Edition, Saunders College
Publishing.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M L L M M L
CO2 H M L L L M M L
CO3 H M L L L M M L
CO4 H L L L L M M L
CO5 H M M L L M M L

H-High; M-Medium; L-Low

 ANALYTICAL TECHNIQUES

COURSE CODE : 18BCHC02 L T P C

Hours
3 1 0 4

MARKS : 100
COURSE
OBJECTIVES : The objective of this course is to understand the working
principles, instrumentation and applications of the instruments
in various disciplines of biological sciences

COURSE OUTCOMES (CO)

After completion of the course, the students will be able,
CO1 to explore the basic concepts of pH, buffers and the types of various
electrochemical cells and its application. The students will also be able to
identify and understand the principle components of a light and electron
microscope with biological applications.
CO2 to explain the principles of the liquid and gas chromatography as well as electro-
migration techniques and evaluate strengths and limitations of the most important
chromatographic separation and detection methods. Be able to define radioactivity
and use them for various biological applications including handling of biohazards.
CO3 to understand how electrophoresis facilitates the separation of molecules based on
various principles of electrophoresis? and be familiar with the types
of electrophoretic gels and their uses.
CO4 to understand the principles of spectroscopy and to analyse and interpret
spectroscopic data collected by the methods discussed in the course. Will be able to
study molecular interactions by choosing suitable spectroscopic methods and
interpreting corresponding data
CO5 to assimilate the principles and applications of centrifuge. Employ the knowledge for
the separation of biomolecules/cells/organelles by selecting appropriate
centrifugation techniques.

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I Electrochemical Principles, electrochemical cells - pH, K1,K2, 13
techniques and Henderson - Hasselbalch equation, buffer K3
Microscopy capacity, pH measurement, glass
electrode, oxygen electrode - principle
and application. Biosensors. Microscopy -
bright field, darkfield, fluorescence and
 phase contrast microscope. Scanning and
transmission electron microscopy.
II Chromatograph Principle, Instrumentation and K1,K2, 12
y& applications- Paper, Thin layer, Ion K3
Radioisotope Exchange, gel filtration, Affinit y
techniques chromatography, HPLC, RF-HPLC,
HPTLC, FPLC, Chromatofocusing,
capillary electrochromatography

Measurement of radioactivity – solid and

liquid scintillation counting, scintillation
cocktails and sample preparation,
Autoradiography, applications of
radioisotopes in biology, radiation
hazards and safe disposal of radioactivit y
waste.
III Electrophoresis Principle, Instrumentation and K1, K2, 13
applications - General principle, K3
migration of charged particle in an
electric field, factors affecting mobility,
Electrophoresis of proteins - native-
PAGE, SDS-PAGE, 2D-PAGE, gradient
gels, isoelectric focusing gels, detection,
estimation & recovery of proteins in gels;
electrophoresis of nucleic acids - agarose
gel electrophoresis, pulse field
electrophoresis, capillary electrophoresis,
Zymography.
IV Spectroscopy Principle, Instrumentation and K1, K2, 12
applications - Atomic absorption K3
spectroscopy and Atomic emission
spectroscopy , UV -Visible,
Spectrofluorimetry, Nephlometry,
Turbidometry, Luminometry, Infra Red,
Electron Spin Resonance, Nuclear
Magnetic Resonance, Mass
Spectrophotometry,
V Centrifugation Basic principles of sedimentation; types K1, K2, 15
of centrifuge; types of rotor; preparative K3
and analytical centrifugation - types and
its applications, CsCl density gradient
and sucrose gradient centrifugation –
principle, applications, determination of
relative molecular mass – sedimentation
velocity and sedimentation equilibrium

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES:

Text Books
1. Wilson,K. and Walker,J. 2010. Principles and Techniques of Biochemistry and
Molecular Biology, 7 t h Edition , Cambridge University. Press.
2. Upadhyay,A. Upadhyay,K. and Nath,N. 2016. Biophysical Chemistry: Principles
and Techniques, 4th Edition, Himalaya Publishing. 11 th Edition
3. Sharma,B.K. 2014. Instrumental Methods of Chemical analysis, Krishna
Prakashan Ltd.

Reference Books
1. Skoog.D, Holler F and Crouch S. 2016. Principles of Instrumental Analysis, 7th
Edition, Cengage Learning custom publishing.

2. Boyer,R. 2009. Modern Experimental Biochemistry, 3rd Edition, Pearson India.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L M L L L M L
CO2 H L M L L M M L
CO3 H M M L M L M L
CO4 H L M L M M M L
CO5 H L M L L L M L

H-High; M-Medium; L-Low

 ADVANCED ENZYMOLOGY

COURSE CODE : 18BCHC03 L T P C

Hours
3 1 0 4

MARKS : 100
COURSE
OBJECTIVES : To understand the classification, kinetics, mechanism of
action, regulation and applications of enzymes.

COURSE OUTCOMES (CO)

After completion of the course, the students will be able to,
CO1 Characterize the enzymes in each enzymatic class, examples of such enzymes and
their isolation and purification procedures in practice. Role of coenzymes in the
activity of enzymes will be thoroughly understood by the students. Students will be
able to differentiate non-protein and protein enzymes and understand the mechanism
of multienzyme systems in detail.
CO2 Understand the concepts of active site of enzyme and their elucidation along with the
basic mechanism of enzyme catalysis with specific examples
CO3 Assess the relationship between properties and structure of the enzymes, kinetics of
enzymatic reactions and their inhibition with specific examples
CO4 Relate the regulatory mechanisms of enzyme activity which involve in the
maintenance of body’s homeostasis
CO5 Choose the correct enzymes for application in various industries by realizing their
current and future potential

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I Classification, Enzyme – Nomenclature and K1,K2 13
Coenzymes and classification of enzymes. General
Purification properties of enzymes: effect of pH,
substrate and temperature on enzyme
catalysed reactions. Coenzymic action
of NAD, FAD, TPP, PLP, Biotin,
CoA, folic acid and lipoic acid.
Purification of enzymes - Methods to
isolate and purify enzymes, activit y
units, Specific activity. Multienzyme
complex : Mechanism of action and
regulation of pyruvate dehydrogenase
 & fatty acid synthase complexes, Non
protein enzymes – Ribozyme,
Abzymes, DNA enzymes.
II Enzyme Active site - Concept of active site, K1,K2 12
catalysis investigations of active site structure,
use of substrate analogues,
modification using chemical
procedures, site-directed mutagenesis.
Types of catalysis - Acid base
catalysis, electrostatic catalysis,
covalent catalysis and metal ion
catalysis. Mechanism of reaction
catalyzed by enzymes - lysozyme.
Metal activated enzymes and
mettalloenzymes. Role of metal ions
in mechanism – carbonic anhydrase
III Enzyme Kinetics : Pre-stead y state and stead y K1, K2, 13
Kinetics and state kinetics, Michaelis Menten K3
Enzyme kinetics, importance of Vmax, Km,
inhibition Linear transformation - Lineweaver-
Burk plot, Eadie - Hoffstee plot and
Hanes plot. Bisubstrate reactions :
ordered, random, sequential, Ping-
Pong reactions. Enzyme inhibition –
Reversible - competitive, non-
competitive, uncompetitive and mixed
inhibition, irreversible inhibition.
IV Enzyme General mechanisms of enzyme K1, K2, 12
regulation regulation, Allosteric control, K3
Symmetric and sequential modes for
action of allosteric enzymes,
Reversible covalent modification,
proteolytic activation. Feedback
inhibition, feed forward stimulation,
sequential feedback, concerted feed
back, cumulative feedback and
enzyme multiplicity, Enzyme
induction and repression.
V Industrial and Industrial application of K3, K4 15
Clinical carbohydrases, proteolytic enzyme,
applications of lignocellulose degrading enzyme,
enzymes pectin and pectic enzyme.
Applications of enzymes in food and
allied industries : leather, textile,
detergent, paper industries.
Immobilisation of enzymes - methods
and applications. Clinical
Enzymology: Enzyme and
isoenzymes in diagnosis –
Phosphatases, transaminases, LD, CK,
 amylase and cholinesterase. Enzymes
as thrombolytic agents, anti-
inflammatory agents, debriding
agents, digestive aids, therapeutic
enzymes.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES:

Text Books
1. Palmer,T. 1995.Understanding enzymes, 4 th Edition, Prentise Hall.
2.Allan Svendsen. 2016. Understanding Enzymes: Function, Design, Engineering
and Analysis. Pan Standford.
3. Price,N.C. and Stevens,L. 1999. Fundamentals of Enzymology, 3 rd Edition,
Oxford University Press.
4. Berg,J.M. et al., 2012. Biochemistry, 7 th Edition, W. H. Freeman & Co.

Reference Books
1. Walsh,G. 2014. Protein Biochemistry and Biotechnology, 2 nd Edition, John Wiley
and Sons Ltd.
2. Chapline,M.F. and Buke,C. 1990. Enzyme technology, 1 st Edition, Cambridge
University Press.
3. Burtis,C. and Bruns,D. 2014. Teitz Fundamentals of Clinical Chemistry, 7 th
Edition, Elsevier.
4. Nelson,D.L. and Cox,M.M. 2017. Lehninger Principles of Biochemistry, 7 th
Edition, W.H. Freeman & Co.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L M L L L M L
CO2 H L L L L M M L
CO3 H L M L M L M L
CO4 H L M L M M M L
CO5 H L M L L L M L

H-High; M-Medium; L-Low

 CELL BIOLOGY AND PHYSIOLOGY

COURSE CODE : 18BCHC04 L T P C

Hours
3 1 0 4

MARKS : 100

COURSE
OBJECTIVES : At the end of the course learners will be able to understand the
structure of membrane, transport mechanism, cell junctions and
adhesion molecules.

COURSE OUTCOMES (CO)

CO1 Understand the structure of membrane. Understand how small and large molecules
transported across a membrane by transport system. Understand the primary
mechanisms by which cells import and export macromolecules.
CO2 Understand the role of cell junctions, cell adhesion molecules and extracellular
matrix components.
CO3 Learn the general characteristics and functions of blood. Acquire the knowledge of
heart and its functions.
CO4 Learn the composition, functions and functions of digestive system. Describe the
structure of organs of excretory system. Learn the role of kidneys and hormones in
their maintenance.
CO5 Learn the structure and functions of nervous system. Study the composition and
metabolic adaptation of brain. Describe the structure of muscles and muscle
contraction.
Analyse the organization amd processes of muscular system.

SYLLABUS

Unit Unit title Intended Learning chapters Knowle Hours

dge of
domain Instru
ction
I Membrane Overview of membrane protein – peripheral, K1,K2 12
structure and integral and fluid mosaic model. Membrane
transport transport: Types, Diffusion - passive and
facilitated. General classes of transport
systems – Uniport, symport, antiport. Active
transport – Primary and secondary, the P-
type ATPase (Na + K + - ATPase), F-type
ATPases (ATP synthases), ABC transporters,
ionophores, aquaporins, ion channels
(ligand-gated and voltage-gated).
II Cell junctions, Major classes of cell junctions – anchoring, K1,K2 12
cell adhesion tight and gap junctions. Major classes of cell
 and ECM adhesion molecules (CAMs) – cadherins,
integrins. The extracellular matrix of
epithelial and nonepithelial tissues. ECM
components – collagen, elastin, fibrillin,
fibronectin, laminin and proteoglycans and
tubulins.
III Blood and Composition and functions of blood and K1, K2 14
circulation plasma. Blood groups. Blood coagulation -
mechanism, fibrinolysis, anticoagulants.
Hemoglobin - structure, abnormal types,
anemia. Structure of heart, cardiac cycle,
heart sounds, E.C.G vasomotor circulation,
coronary circulation, blood pressure, spleen,
lymph, normal composition and function of
lymph - role of different lymph cells.
IV Digestive and Digestive secretions - composition, functions K1, K2 13
Excretory and regulation of saliva, gastric, pancreatic,
system intestinal and bile secretions. Digestions and
absorption of carbohydrates, lipids, proteins
and nucleic acids. Excretory system -
structure of nephron. Formation of urine -
glomerular filtration, tubular reabsorption of
glucose, water and electrolytes, tubular
secretion. Regulation of water and
electrolyte balance, role of kidneys and
hormones in their maintenance
V Neuromuscula Structure and function of nerves, neurons, K1, K2 14
r function resting and action potential, transmission of
nerve impulses, synaptic transmission,
compounds affecting synaptic trans mission,
neuromuscular junction, composition and
functions of cerebrospinal fluid, brain -
chemical composition and metabolic
adaptation, neurotransmitters and cAMP,
biochemical aspects of learning and memory,
enkephalins and endorphins. Structure of
muscle cells and muscle contraction,
molecular organization of muscle, proteins of
contractile element - their organization and
role in contraction, energy for contraction.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
REFERENCES:

Text Books

1. Alberts,B. et al., 2008. Molecular Biology of the Cell, 5 th Edition, Garland

Publishing Co.

2. Guyton,A.C. and Hall,J.E. 1996. Human Physiology and Mechanisms of Disease,

6 th Edition, Saunders.
Reference Books

1. Lodish et al. 2016. Molecular Cell Biology, 7 t h Edition, W.H. Freeman and Co.

2. Cooper,G.M. and Hausman,R.E. 2013. The Cell: A Molecular Approach, 6 th

Edition, Sinauer Associates, Inc.

3. Chatterjee,C.C. 1985. Human Physiology, 11 t h Edition. Medical Allied Agency

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L M M L L M L
CO2 H L M M L M M L
CO3 H L M M L L M L
CO4 H L M M L M M L
CO5 H L M M L L M L

H-High; M-Medium; L-Low

 CORE PRACTICAL I
BIOCHEMICAL TECHNIQUES AND ENZYMOLOGY

COURSE CODE : 18BCHP01 L T P C

Hours
MARKS : 100 - - 5 4

COURSE
OBJECTIVES : At the end of the course learners will be able to qualitatively and
quantitatively identify the biomolecules present in the given sample

1. Preparation of normal, molar and percentage solution

2. Estimation of fructose in fruits
3. Estimation of calcium in milk
4. Isolation and estimation of starch from potato
5. Isolation and estimation of ascorbic acid from citrus fruit
6. Estimation of β-carotene from carrot
7. Estimation of total free amino acids in plant tissues
8. Estimation of reducing sugars
9. Estimation of protein
10. Estimation of iron
11. Thermal denaturation of DNA.
12. Isolation, purification and characterization of peroxidase or amylase
13. Separation of amino acids by circular and ascending paper chromatography
14. Mitosis and meiosis

OUTCOMES
The students will be acquainted with hands-on knowledge in the qualitative and
quantitative analysis of biomolecules in the given samples.
 INTERMEDIARY METABOLISM

COURSE CODE : 18BCHC05 L T P C

Hours
3 1 0 4

MARKS : 100

COURSE
OBJECTIVES : To understand the various metabolic pathways operating in living
cells with special emphasis on carbohydrate, lipid, amino acid,
nucleic acid metabolism and the electron transport chain.

COURSE OUTCOMES (CO)

After completion of the course, the students will be able,
CO1 To demonstrate an understanding of the metabolic pathways - the energy-
yielding and energy requiring reactions in life
CO2 To demonstrate an understanding of the diversity of metabolic regulation.
CO3 To emphasis the unique role in metabolism for life existence
CO4 To provide conceptual theoretical knowledge
CO5 To relate various metabolic connectivity and its control

SYLLABUS

Unit Unit title Intended learning chapters Knowledge Hours of

domain instruction
I. Bioenergetics Free energy and entropy. Phosphoryl group K1 & K2 18
and transfers and ATP. Enzymes involved in
Biological redox reactions. The electron transport
Oxidation chain - organization and role in electron
capture. Oxidative phosphorylation -
Electron transfer reactions in mitochondria.
F1F0 ATPase - Structure and mechanism of
action. The chemiosmotic theory. Inhibitors
of respiratory chain and oxidative
phosphorylation - Uncouplers and
ionophores. Regulation of oxidative
phosphorylation. Mitochondrial transport
systems - ATP/ADP exchange, malate /
glycerophosphae shuttle, creatine -
phosphate shuttle.
 II. Carbohydrate Glycolysis and gluconeogenesis - K1 & K2 16
metabolism regulation. The citric acid cycle and
regulation. The pentose phosphate
pathway. Metabolism of glycogen and
regulation. Metabolism of galactose and
fructose. The glyoxylate cycle. Cori cycle.
Futile cycles, anaplerotic reactions
III. Lipid Biosynthesis of fatty acids - fatty acid K1 & K2 16
Metabolism synthase complex, regulation of
lipogenesis. Oxidation of fatty acids – role
of carnitine in fatty acid transport, α, β and
ω oxidation. Metabolism of triglycerides,
phospholipids and sphingolipids.
Cholesterol - Biosynthesis, regulation,
transport and excretion. Metabolism of
lipoproteins. Eicosanoid metabolism
IV. Amino Acid, Overview of biosynthesis of 20 amino K4& K6 15
Purine and acids found in proteins - Amino acids from
Pyrimidine Ser family (gly), pyruvate family (leu),
metabolism aspartate family (lys), glutamate family
(gln), aromatic amino acid family (trp) and
histidine family (his). Catabolism of amino
acid nitrogen- transamination, deamination,
ammonia formation and the urea cycle.
Catabolism of carbon skeletons of amino
acids. Conversion of amino acids to special
products. Metabolism of purines - De novo
and salvage pathways for biosynthesis.
Purine catabolism. Biosynthesis and
catabolism of pyrimidines.
V. Porphyrins, Biosynthesis and degradation of porphyrins K1 & K2 15
Minerals and and heme. Minerals : sources, absorption,
metabolic metabolism, biological roles and clinical
integration significance of calcium, phosphate and
magnesium. Trace elements: absorption,
metabolism, storage and transport of iron,
copper, zinc, selenium. Manganese, cobalt
and fluoride. Integration of metabolism

REFERENCE:

Text Books

1. Murray et al., 2012. Harper’s Biochemistry, 30 th Edition, McGraw Hill Medical

Publication.
2. Nelson,D.L. and Cox,M.M. 2013.Lehninger Principles of Biochemistry, 6 th Edition,
W.H. Freeman & Co.
3. Berg,J.M. et al., 2012. Biochemistry, 7 th Edition, W. H. Freeman & Co.

Reference Books
1. Voet,D. et al., 2012. Fundamentals of Biochemistry: Life at the Molecular level,
4 th Edition, John Wiley and Sons.
2. Zubey,G.L. 1998. Biochemistry, Wm.C. Brown Publishers.
3. Garrett,R. and Grisham,C. 2010. Biochemistry, 4 th Edition, Saunders College
Publishing.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L M M L L M L
CO2 H L M M L M M L
CO3 H L M M L M M L
CO4 H L M M L L M L
CO5 H L M M L L M L

H-High; M-Medium; L-Low

 PLANT BIOCHEMISTRY

COURSE CODE : 18BCHC06 L T P C

Hours
3 1 0 4

MARKS : 100

COURSE
OBJECTIVES : To understand the plant cell wall structure, biochemical processes
that take place in plant such as plant metabolic processes,
photosynthetic reactions, plant hormones, and plant secondary
metabolites

COURSE OUTCOMES (CO)

After completion of the course, the students will be able,
CO1 To explain the plant cell wall structure and to understand the plant nuclear, plastid
genome organization and explain the biogenesis of organells
CO2 To explain the basic concepts in photosynthesis and its regulation
CO3 to understand different biogeocyles and its impact on earth. The basic knowledge on
mineral nutrition in plant health and deficiencies will also be understood.
CO4 To evaluate the impact of hormones in plant growth, flowering and
maintenance.
CO5 To imbibe the mechanism of action of plant defences, antiodixant system in plant
defenses and photochemistry of plants.

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I Plant cell wall Plant cell wall - Structure and function. Water K1,K2, 13
and genome uptake and movement – diffusion, osmosis, K3
organization aquaporins. Plant genome organization: Plant
nuclear and plastid genome organization.
Biogenesis of organelles - developlment of
chloroplast. Interaction between nuclear and
organellar genome
II Photosynthesis Photosynthesis - Structure of organelles involved K1,K2, 12
and its in photosynthesis in plants and bacteria. Proton K3
regulation gradients and electron transfer in chloroplasts of
plants. Light receptors - chlorophyll, light
harvesting complexes, bacteriorhodopsin,
rhodopsin as ion pump. Photosystems I and II.
The Hill reaction, Photophosphorylation and
reduction of CO 2 , C 3 , C 4 and CAM metabolism,
light and dark reactions. Light activation of
enzymes, regulation of photosynthesis.
Photorespiration.

III Mineral Mineral Nutrition - Biogeo cycles (Carbon, Nitrogen K1, K2, 13
nutrition and Sulphur), Nitrate assimilation: structural features K3
of nitrate reductase and nitrite reductase,
incorporation of ammonia into organic compounds,
regulation of nitrate assimilation. Sulphur assimilation
in plants. Nutrient absorption and translocation,
Nutrient functions in growth and development,
Nutrient deficiency symptoms, toxicity problems
IV Phytohormones Phytohormones : Auxins, cytokinins, Abscisic K1, K2, 12
acid, Gibberellins, ethylene- Structure, K3
physiological function and metabolism. Plant
movement, apical dominance. Stomatal
movements and morphogenesis. Photoperiodism
and vernalization – flower induction, initiation
and development.

V Plant defense Biological rhythm in plants, plant defenses, K1, K2, 15

system and environmental and genetic control, Antioxidative K3
phtochemistry defence system in plants – reactive oxygen
species and their generation, enzymic and non-
enzymic components of antioxidative defence
mechanism. Special features of secondary plant
metabolism-phytochemistry of plants. Plant tissue
culture and its applications.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
REFERENCES:

Text Books
1. Heldt,H.W. and Piechulla,B. 2016. Plant Biochemistry, 4 th Edition, Academic Press.
2. Heldt,H.W. 2004. Plant Biochemistry, 3 rd Edition, Academic Press.
3. Buchannan,B. et al, 2015. Biochemistry and Molecular Biology of Plants, 2 nd
revised Edition, Wiley.
4. Verma S.K. and Verma Mohit. 2007. Text book of Plant Physiology, biochemistry
and Biotechnology, 6 th Edition, S. Chand.
5. Goodwin and Mercer. 2005.Introduction to Plant Biochemistry.2 nd Edition, CBS.

Reference Books
1. Dey. 2013. Plant Biochemistry, 1 st edition, Elsevier.
2. Dey,P.M. and Harborne,J.B. 1997. Plant Biochemistry, 1 st Edition, Academic Press.
3. Lea,P.J. and Leegood,R.C. 1999. Plant Biochemistry and Molecular Biology, 2 nd
Edition, Wiley.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L L L L L M L
CO2 H L L L L M M L
CO3 H L L L L L M L
CO4 H L L M L M M L
CO5 H L L M L L M L

H-High; M-Medium; L-Low

 MOLECULAR BIOLOGY

COURSE CODE : 18BCHC07 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : To understand the basic structure and functioning of the genetic
material, knowledge on the activity of genes and genomes,
molecular mechanisms of DNA replication, repair, recombination,
transcription, protein synthesis and gene regulation.

.
COURSE OUTCOMES (CO)
CO1 Molecular biology gives an in-depth knowledge of biological processes
through the investigation of the underlying molecular mechanisms.
CO2 Describe the processes of replication, repair and recombination
CO3 Understanding the underlying process of prokaryotic transcription and
regulation
CO4 Explain the mechanism of eukaryotic transcription and regulation
CO5 Provides the basics of genetic code, translation and targeting

SYLLABUS
Unit Unit title Intended Learning chapters Knowled Hours
ge of
domain Instruct
ion
I Chromatin and Central dogma of Molecular biology. Structure of K1,K2 13
Genome the bacterial nucleoid - The E.coli chromosome
and DNA-binding proteins. Plasmids-
classification and properties. The eukaryotic
chromatin- nucleosomes, 30 nm fiber and
chromatin loops. Organization of chromatin
structure. Genome complexity- genome size, C-
value paradox, coding and non coding DNA,
typical structure of protein-coding genes in
prokaryotes and eukaryotes. Introns and exons and
repetitive DNA (SINES, LINES, simple sequence
repeats - satellite, minisatellite and
microsatellite). gene duplication and pseudogenes
.Organelle genomes- mitochondria and
chloroplast.

II Replication, DNA replication in prokaryotes and eukaryotes K1,K2 12

 Repair and (helicases, SSB, topoisomerases, DNA
Recombination polymerases and DNA ligase), Telomeres,
telomerases and end replication. Inhibitors of
replication. DNA repair mechanisms - Nucleotide
excision repair, base excision repair, mismatch
repair, double-strand break repair, recombination
repair and SOS response. Recombination –
Homologous recombination, site specific
recombination. Transposons and mechanism of
transposition (elementary details).

III Prokaryotic E.coli RNA polymerase, Promoter sequence in K1, K2 13

Transcription E.coli, Initiation, elongation and termination. Rho
and Regulation dependent and Rho independent termination.
Inhibitors of transcription. Post-transcriptional
processing of rRNA and tRNA. Regulation of
transcription in prokaryotes – lac operon and
trytophan operon.

IV Eukaryotic RNA polymerases - structure, RNA pol I, II and K1, K2, 12

Transcription III, transcriptional factors, Transcription initiation
and Regulation by RNA polymerase I, II and III. Transcriptional
regulation in eukaryotes - steroid hormone
receptors and phosphorylation. Post
transcriptional processing of mRNA, rRNA and
tRNA. Alternative splicing, RNA editing,
Antisense RNA, Micro RNAs and RNA
interference.

V Genetic Code, Genetic code - salient features. Mitochondrial K1,k2, 15

Translation and genetic code. Mutations– point mutations and K3
Targeting frame shift mutations. Suppressor mutations –
nonsense and missense suppression. Mechanism
of protein synthesis in bacteria and eukaryotes-
amino acid activation, initiation, elongation and
termination. Inhibitors of protein synthesis. Co
and post-translational modifications. Protein
targeting to membranes, nucleus, mitochondria,
lysosomes, signal sequence hypothesis, Protein
degradation- the ubiquitin pathway. Protein
folding- (elementary details).
Program specific attributes
Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES:

Text Books
1. Lodish et al. 2012. Molecular Cell Biology, 7 th Edition, W.H. Freeman and Co.
2. Weaver,R.F. 2011. Molecular Biology, 5 th Edition, WCB McGraw Hill, Higher
Education.
3. Karp,G. 2009.Cell and Molecular Biology, 6 t h Edition, John Wiley & Sons, Inc.

Reference Books
1. Alberts,B. et al., 2008. Molecular Biology of the Cell, 5 th Edition, Garland
Publishing Co.
2. Watson,J.D. et al., 2013. Molecular Biology of the Gene, 7 th Edition, Pearson
Education.
3. Lewin,B. 2007. Genes IX, 9 th Edition, Jones and Bartlett Publishers.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L L M L L M L
CO2 H L L M L L M L
CO3 H L L L L L M L
CO4 H L L M L L M L
CO5 H L L L L L M L

H-High; M-Medium; L-Low

 CORE PRACTICAL II
MOLECULAR AND MICROBIAL TECHNIQUES

COURSE CODE : 18BCHP02 Hours L T P C

MARKS : 100 -- - 5 4
COURSE
OBJECTIVES : This course is designed to provide hands-on training in molecular
and microbial techniques.

1. Isolation and estimation of DNA

2. Isolation and estimation of RNA
3. Estimation of phosphorus
4. Estimation of chlorophyll in leaves
5. Estimation of phenols in plant tissues
6. Estimation of peroxidase in plant tissues
6. Plant tissue culture (Demo)
Callus induction. Initiation of suspension cultures, Regeneration of shoot and root
from callus culture
7. Animal tissue culture (Demo)
Preparation and sterilization of media, Filter sterilization of media, Primary cell
culture – trypsinisation, passaging, staging, cell lines, counting – vital staining,
Cytotoxicity and viability assay
8. Isolation of pure culture - Serial dilution, pour plate, spread plate, streak plate
9. Staining techniques - Simple, differential
10. Separation of lipids by TLC
11. Separation of proteins by SDS-PAGE
12. Agarose gel electrophoresis of DNA

OUTCOMES

After the completion of this course the students will be able to understand and gain practical
experience in molecular and microbial techniques
 GENETIC ENGINEERING

COURSE CODE : 18BCHC08 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : To familiarize the students with the basic concepts in genetic
engineering; to acquaint the students to versatile tools and
techniques employed in genetic engineering and recombinant
DNA technology; and to appraise them about applications of
genetic engineering.

COURSE OUTCOMES (CO)

CO1 The student will have knowledge of tools and strategies used in genetic
engineering.
CO2 Understanding the application of genetic engineering techniques in basic and
applied research.
CO3 To provide the ethical values and nurturing applicablility of conserved
genetic traits
CO4 To impact knowledge latest updation and application of genetic engineering
CO5 To motivate and create interest to uptake genetic engineering for research

SYLLABUS

Unit Unit title Intended learning chapters (K1,K2) Knowledge Hours of

domain instructio
n
I. Restriction Basic steps in gene cloning. Type II Restriction K1 & K2 18
endonucleas endonucleases- nomenclature and types of
es, cloning cleavage. Cloning vectors: plasmids (pBR322
vectors, and and pUC), phage vectors (λ), cosmids,
ligation phagemids, BACs and YACs. Methods of
ligation of insert and vector DNA molecules:
cohesive end method, homopolymeric tailing,
blunt-end ligation, linkers and adapters.

II. Gene Gene transfer methods: calcium phosphate K2,K3 16

transfer coprecipitation, electroporation, lipofection,
methods - viruses, microinjection. Choice of host organisms
cloning & for cloning. Construction of genomic and
screening cDNAlibraries . Cloning strategies- genomic
strategies cloning, cDNA cloning. Differences between
genomic and cDNA libraries. Screening of
recombinants: marker inactivation (antibiotic
 resistance, blue-white selection), colony
hybridization, immunoscreening, screening for
protein activity.

III. Expression Factors affecting expression of cloned genes. K1&K2 16

systems Expression of eukaryotic genes in bacteria-
expression vector, promoters, industrial protein
production. Fusion proteins, strategies to enhance
protein stability, secretion and metabolic load.
Expression in eukaryotic cells: Expression in
yeast- yeast vectors, GAL system. Baculovirus
and Mammalian expression systems (brief
account). Tagged proteins and secretion signals.
Reporter genes- types and uses.

IV. Gene Extraction and purification of nucleic acids. K1,K3,K4 16

Manipulatio Probes: radioactive and nonradioactive. Blotting &K5
n techniques: Southern, northern, and western.
Techniques Principle and applications of DNA
fingerprinting, DNA footprinting in situ
hybridization, PCR, RT-PCR, real-time qPCR.
DNA Sequencing: Automated sequencing. Next-
generation sequencing. Site-directed mutagenesis
(SDM): cassette and oligonucleotide-directed
mutagenesis. PCR-based methods. Protein
engineering by directed evolution and DNA
shuffling. Hazards and safety aspects of genetic
engineering.

V. Gene Transformation, co-transformation, selectable K1 & K2 16

targeting & markers, reporter genes. Transgenic animals -
Metabolite methods of production gene knock out in
Engineering transgenic mice. Transgenic animals as models of
human disease. Application of transgenic mice,
animal bioreactors (Pharm animals).Antisense
RNA technique, Harbicide resistance. Methods of
gene transfer in plants-Agrobacterium-mediated
transformation and particle gun method.
Transgenic plant technology-development and
applications.
REFERENCE:

Text Books
th
1. Brown,T.A. 2010. Gene cloning and DNA analysis: An introduction, 6 Edition,
Wiley-Blackwell Publishers.
2. Primrose,S.B. and Twyman,R. 2006. Principles of Gene Manipulation and
Genomics, 7 th Edition, Oxford University Press.
3. Glick,B.R. and Pasternak,J.J. 2009. Molecular Biotechnology - Principles and
Applications of Recombinant DNA, 4 th Edition, ASM Publishers.

Reference Books
1. Strachan,T. and Read,A.P. 2003. Human Molecular Genetics, 3 rd Edition, Garland
Science Publishers.
2. Watson,J.D. et al., 2007. Recombinant DNA-Genes and Genomes: A short course, 3 rd
Edition, Cold Spring Harbor Laboratory Press.
3. Winnacker,E.L. 1987. From Genes to clones, 1 st Edition, Wiley-Blackwell
Publishers.
4. Nicholl,D.S.T. 2008. An introduction to Genetic Engineering. 3 rd Edition,
Cambridge University Press

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M M M L M L
CO2 H M M M M M M L
CO3 H M M M M L M L
CO4 H M M M M M M L
CO5 H M M M M L M L

H-High; M-Medium; L-Low

 ADVANCED CLINICAL BIOCHEMISTRY

COURSE CODE : 18BCHC09 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : To impart knowledge about the biochemical basis of various
diseases and disorders, and to study various diagnostic and
therapeutic methodologies available for diseases and disorders.

COURSE OUTCOMES (CO)

CO1 To have a basic knowledge on collection of samples, role of preservatives, time of its
additions, need of its addition, and also various procedures involved in collection of
clinical samples like blood, urine, stool, CSF, amniotic fluid as well as purpose of
collection, biochemical test that could be carried out in the samples.
CO2 To have a critical understanding on In born errors of metabolism. And its causative
factors like genetic defect in specific key metabolic enzymes induced specific
diseases of carbohydrate, lipid, protein, purine and pyrimidine metabolism.
CO3 Enzymatic assay protocols that could help one to diagnose the specific illness like
hepatobiliary diseases by comparing with their normal values and by knowing
cusative factors .
CO4 Understand the test available for gastric, liver, pancreas function in order to assess
the laboratory results obtained as well as to interpret them.
CO5 To have a better in-depth knowledge on diagnosis using biochemical parameters,
complications, management of diseases like Diabetes mellitus, Atherosclerosis,
cancer.

SYLLABUS

Unit Unit title Intended learning chapters (K1,K2) Knowledge Hours of

domain instructio
n
I. Specimen Collection of blood by various methods, K1,K2,K3 15
collection anticoagulants. Collection of urine - Timed urine
and specimens, urine preservatives. Stool – chemical
processing examination and clinical significance. CSF –
composition and collection, chemical
examination and infections and spinal cord
infections.Amniotic fluid : Origin, collection,
composition and analysis of amniotic fluid
Automation in the clinical biochemistry:
Precision, reliability, reproducibility and other
factors in quality control.
II. Inborn Disorders of carbohydrate metabolism – K1,K2,K3 15
 errors of glycogen storage diseases, galactosemia, fructose
metabolism intolerance and fructosuria. Disorders of lipid
metabolism - Lipid storage diseases, fatty liver
and lipoproteinemias. Disorders of amino acid
metabolism – Aminoaciduria, phenylketonuria,
Hartnup disease, alkaptonuria, albinism,
cystinuria, cystinosis, homocystinuria and maple
syrup urine disease. Disorders of purine,
pyrimidine and porphyrin metabolism-
Hyperuricemia, Hyporuricemia and gout, orotic
aciduria, porphyrias – Erythropoietic and hepatic.
III. Clinical Serum enzyme activities in diseases - Principle K1, K2, 11
enzymology and assay of transaminases, phosphatases, K3
isocitrate dehydrogenase, 5’ nucleotidase, ά-
hydroxybutyrate dehydrogenase, ceruloplasmin,
γ-glutamyl transpeptidase, creatine kinase.
lactate dehydrogenase, amylase, lipase, choline
esterase. Enzyme patterns in disease –
hepatobiliary disease, myocardial infarction
IV. Hepatic, Normal structure and functions of liver, diseases K1, K2, 12
pancreatic of the liver, hepatitis types, cirrhosis, liver K3
and renal function tests, disorders of bilirubin metabolism.
functional Pancreatic and gastric function tests – peptic
tests ulcer Renal function tests - Biochemical findings
in glomerulonephritis, acute and chronic renal
failure, nephritic syndrome, nephrolithiasis.
Normal and abnormal constituents of urine.
V. Diabetes, Blood glucose homeostasis-Role of tissues and K3, K4, 12
Atherosclero hormones. Diabetes mellitus–classification, K5
sis and metabolic abnormalities, diagnosis and
Cancer management, acute and long-term complications.
Atherosclerosis – risk factors, biochemical
findings and management. Cancer – Benign and
malignant tumour, tumour markers

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
REFERENCES:

Text Books

1. Burtis,C. and Bruns,D. 20. Teitz Fundamentals of Clinical Chemistry, 7 th

Edition, W.B. Saunders Company.
2. Devlin,T.M. 2010. Text book of Biochemistry with Clinical Correlation, 7 th
Edition, John Wiley and Sons.
3. Varley,H. 1980.Practical Clinical Biochemistry, Volume I and II, 5 th Edition, CBS
Publishers.

Reference Books
1. Mayne,P.D. 1994. Clinical Chemistry in Diagnosis and Treatment, 6 th Edition,
Hodder Arnold Publication.
2. Marshall,W.J. and Bangeit, S.K. 1995. Clinical Biochemistry - Metabolic concepts
and Clinical aspects, Churchill Livingstone.
3. Guyton,A.C. and Hall,J.E. 2015. Text Book of Medical Physiology, 13 th Edition,
Saunders

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M M H H M L
CO2 H M M M M H M L
CO3 H M M M H H M L
CO4 H M M M H H M L
CO5 H M M M M H M L

H-High; M-Medium; L-Low

 IMMUNOLOGY

COURSE CODE : 18BCHC10 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : The candidate will gain knowledge about the molecular and cellular
interactions and principles of the immune system, B & T cells
maturation and specific response.

COURSE OUTCOMES (CO)

CO1 To provide students with knowledge on how the immune system works. A
description of cells involved in the immune response either innate or acquired.
Understand the contributions of the organs. Provide basic knowledge of the
organization and function of the immune system.
CO2 Understand the antibodies and immunoglobulins, Be able to distinguish and
characterize antibody isotypes and functions.
CO3 Understand the significance of MHC molecules in terms of immune response. Be
able to describe lymphocyte development and their expression of receptors,
Compare and contrast the origin, maturation process.
CO4 Comprehend the over reaction by our immune system leading to hypersensitive
conditions and its consequence.
CO5 Gain knowledge about immunologic processes governing graft rejection and
therapeutic modalities for immunosuppression in transplantation. Understand the
properties of tumour antigens, immune response to tumours.

SYLLABUS
Unit Unit title Intended Learning chapters Knowled Hours
ge of
domain Instruc
tion
I Innate and Immune cells, structure and function. K1,K2 13
adaptive Erythropoiesis, growth factors, regulation of
immunity, hematopoiesis, cells. clinical uses of stem cells,
comparative Null cells, granulocytes, adhesion molecules
immunity cells Organs of the immune system; primary and
secondary organs
Lymphoid cells: Lymphoblast’s, CD antigens, B
cell receptors. T cell membrane molecules.
II Antigens B cell epitopes, T cell epitopes, Haptens- viral K1,K2 12
and bacterial antigens, factor-influencing
immunogenicity, adjuvant technology.
Immunoglobulins: domains, allotypes, Isotypes
and Idiotypes, antigenic determinants on
 Immunoglobulins. Immunoglobulins superfamily.
Monoclonal antibodies: Formation and selection
of hybrid cells, production, clinical uses,
Abzymes.
III MHC Organization, MHC molecules and genes, cellular K1, K2 13
distribution, regulation of MHC and immune
responsiveness, MHC and susceptible deficiency
diseases. Antigen processing and presentation.
T-cell: Receptor complex structure, T-cell
maturation, activation and differentiation. Cell
death and T-cell population.
B-cell: Receptor complex structure, T-cell
maturation, activation and differentiation.
Complement activation: Pathways, regulation of
complement system, Biological consequences of
complement activation, complement deficiencies.
Antigens - Antibody interaction: In vivo - cross
reactivity, In vitro: precipitants, agglutinants.
IV Cytokines Structure and function of IL, IFN, TNF, CSF, K1, K2, 12
cytokines receptors, cytokine antagonists, and
cytokines related diseases.
Cell mediated immunity: CTL mediated
cytotoxicity, NK cell mediated toxicity, delayed
type hypersensitivity
Leukocyte mediated immune response: Cell
adhesion molecule, Lymphocyte and neutrophils,
extravasation, mediators of inflammation,
inflammatory process.
Hypersensitivity reactions: Type I, II, III and IV.
Hypersensitivity diseases. Immunity to infectious
diseases: viral - influenza, bacteria – tuberculosis,
parasite – Plasmodium falciparum.
V Transplantation Types, Genetics of transplantation, Graft versus K1,k2, 15
immunology host reaction, tissue matching and K3
immunosuppressive agents, clinical manifestation,
therapy and bone-marrow transplants, organ-
transplants.
Immunodeficiency diseases: B-cell, T-cell, SCID,
Pathogenesis, diagnosis and treatments of AIDS.
Vaccines: Active and passive immunization,
whole organism vaccines, recombinant vector
vaccines, DNA vaccines, synthetic peptide
vaccine, multivalent sub-unit vaccines.
Program specific attributes
Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES:

Text Books
1. Owen,J.A. et al., 2013. Kuby Immunology, 7 th Edition, W.H. Freeman and
Company.
2. Delves,P. et al., 2011. Roitt’s Essential Immunology, 12 th Edition, Wiley-Blackwell
Publishers.

Reference Books
1. Abbas,A.K. et al., 2012. Cellular and Molecular Immunology, Fourth Edition,
Elsevier Saunders Company.
2. Ananthanarayan,R. 2009. Ananthanarayan and Paniker's Textbook of Microbiology
8 th Edition, Universities Press Publishers
3. Virella,G. 2007. Introduction to Medical Immunology, 6 th Edition, CRC Press.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M L M L M M L
CO2 H M L M L M M L
CO3 H M L M L M M L
CO4 H M L M L M M L
CO5 H M L M L M M L

H-High; M-Medium; L-Low

 CORE PRACTICAL III
CLINICAL BIOCHEMISTRY AND GENETIC ENGINEERING

COURSE CODE : 18BCHP04 Hours L T P C

MARKS : 100 -- - 5 4
COURSE
OBJECTIVES : This course is designed to provide hands-on training in clinical
Biochemistry and recombinant DNA techniques.

1. Estimation of blood glucose

2. Estimation of blood Urea
3. Estimation of serum uric acid
4. Estimation of serum creatinine
5. Estimation of serum calcium
6. Estimation of serum phosphorus
7. Estimation of serum Bilirubin – TB, DB
8. Estimation of serum protein, albumin, AG ratio
9. Assay of Alkaline phosphatase
10. Assay of Aspartate amino transferase
11. Isolation of genomic DNA from liver/plant/ bacterial source
12. Isolation of plasmid DNA from bacteria
13. Restriction digestion of DNA
14. Transformation in E.coli
15. PCR demonstration

OUTCOMES

The students will be able to understand and apply the hands-on knowledge gained in
clinical biochemistry and genetic engineering in their future research activites as well
as while establishing clinical laboratories
 DRUG BIOCHEMISTRY AND CLINICAL TOXICOLOGY

COURSE CODE : 18BCHC11 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : This course is designed to provide detailed understanding of the
pharmacological and toxicological aspects of therapeutics and
their diverse modes of drug action.

COURSE OUTCOMES (CO)

CO1 To know the theories and principles of drug action, drug metabolism and
pharmacodynamics.
CO2 To know effects of toxicants on organ system and drug disposition.
CO3 To provide the dynamic effects various drugs
CO4 To distinguish therapeutic and deleterious effects of drug use invivo
CO5 To exactly provide distinct picture of xenobiotics living system.

SYLLABUS
Unit Unit title Intended learning chapters Knowledg Hours of
e domain instruction
I. General Basic principles of drug action- K1 & K2 19
Principles Pharmacokinetics : Absorption, distribution and
elimination of drugs, routes of drug
administration. Pharmacogenetics. Origin of
Drug from plants and animals.
II. Drug General pathways of drug metabolism (different K1, K2 15
metabolism types of reaction in phase I and phase II with
examples), metabolism and excretion of drugs.
Mechanism of drug action, combined effect of
drugs. Factors modifying drug action, tolerance
and dependence
III. Pharmacody receptor concepts, theory, drug receptor K1, K2 17
namics interaction (DRI), Factors affecting DRI,
Cholinergic and anticholinergic drugs,
Adrenergic and adrenergic blockers, General
anesthetics, Local anesthetics. Adverse reactions
to drugs and common drug receptor interactions
IV. Principles of Chemotherapy of microbial diseases, K1, K2 17
therapeutics Chemotherapy of fungal infections,
Chemotherapy of parasitic infections, rational
 use of antibiotics. Application for New Drug
Discovery (NDD) according to Indian Control
Authority and USFDA guidelines. Ethical
considerations in utilizing human subjects for
drug discovery process. Helsinki’s declaration.
V. Toxicology Principles of toxicology and treatment of K1 & K2 12
poisoning. Heavy metals and antagonists. Non
metallic environmental toxicants. Methods
involved in the development of new drugs.
Preclinical toxicological studies. Calculation of
LD 50 and ED 50 . Acute, subacute and chronic
toxicity studies. Irwin profile test, Pre-clinical
pharmacokinetic and dynamic studies. Lipinski’s
rule for drug like molecule, High throughput
screening (in vitro and in vivo) for pre-clinical
pharmacokinetic and pharmacodynamic studies.
REFERENCE:

Text Books
1. Satoskar,R.Set al., 2013. Pharmacology and Pharmacotherapeutics, 23 rd Edition,
Popular Prakasham, Bombay.
2. Williams,D.A. et al., 2008. Foye’s Principles of Medicinal Chemistry, 6 th Edition,
Lippincott Williams & Wilkins.
3. Ghosh,M.N. 1984. Fundamentals of Experimental Pharmacology, 2 nd Edition,
Scientific Book Agency, Kolkatta.

Reference Books
1. Shargel,L.et al., 2012. Applied Biopharmaceutics and Pharmacokinetics, 6 th
Edition, McGraw-Hill Medical,
2. Foreman,J.C. and Johansen,T.J. 1996. Text Book of Receptor Pharmacology,
2 nd Edition, CRC Press.
3. Goodman,L.S. et al., Goodman and Gillman’s the pharmacological basis of
therapeutics, 6 th Edition,, McGraw Hill, 1996.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L L M L M L L
CO2 H L L M L L L L
CO3 H L L M L M L L
CO4 H L L M L L L L
CO5 H L L M L M L L

H-High; M-Medium; L-Low

 CORE PRACTICAL IV
CLINICAL BIOCHEMISTRY AND IMMUNOLOGY

COURSE CODE : 18BCHP04 Hours L T P C

MARKS : 100 -- - 5 4
COURSE
OBJECTIVES : This course is designed to provide hands-on training in clinical
Biochemistry and immunochemical techniques.

1. Estimation of Glutathione peroxidase

2. Estimation of reduced Glutathione
3. Estimation of Vitamin C
4. Estimation of Lipid peroxidation
5. Estimation of triglycerides
6. Estimation phospholipids
7. Estimation total cholesterol
8. Estimation of HDL and LDL cholesterol
9. Immuno diffusion – Single radial and double diffusion
10. Immunoelectrophoresis
11. Rocket immunoelectrophoresis
12. Agglutination tests
13. Serial dilution of ASO titre,VDRL titre

OUTCOMES
The students will have a clear understanding and hands-on experience on the most
practical aspect of clinical biochemistry and immunology
ELECTIVES
 MOLECLAR ENDOCRINOLOGY

COURSE CODE : 18BCHE01 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : To obtain sound knowledge in Hormonal Biochemistry.

COURSE OUTCOMES (CO)

CO1 To provide core principle and concepts of molecular endocrinology to unable to
students understand and acquire knowledge.
CO2 To provide clear under standing and critical interpretations of clinical manifestation.
CO3 To impact the basis theoretical knowledge in molecular endocrine
CO4 Educating and familiarizing the terms and concepts of molecular endocrinenology
CO5 To impact complete idea and knowledge in hormones.

SYLLABUS

Unit Unit title Intended learning chapters (K1,K2) Knowledg Hours

e domain of
instruct
ion
I. Introduction Historical and anatomy aspects of mammalian K1 & K2 19
endocrine system . Classification of hormones and
mechanism of action. Hypothalamic and pituitary
hormones. Hypothalamic releasing factors.
Anterior pituitary hormones: biological actions,
regulation and disorders of growth hormone,
ACTH, gonadotropins and prolactin. Leptin.
Posterior pituitary hormones- biological actions of
vasopressin.Diabetesinsipidus and syndrome of
inappropriate ADH secretion (SIADH) Oxytocin.
Hypopituitarism. Classification, biological action
regulation and disorders of Anterior pituitary
hormones (growth hormone, ACTH,
gonadotropins and prolactin) , Posterior pituitary
hormones (vasopressin, ADH, Oxytocin).

II. Thyroid and Thyroid hormones- synthesis, secretion, K1, K2& 15

Parathyroid regulation, transport, metabolic fate and K4
hormones biological actions. Antithyroidagents.Thyroid
function tests. Hyper and hypothyroidism.
Hormonal regulation of calcium and phosphate
 metabolism.Secretion and biological actions of
PTH, calcitonin and calcitriol. Hypercalcemia and
hypocalcemia. Rickets and osteomalacia.

III. Adrenal Adrenal cortical hormones.Synthesis, regulation, K1, 15

hormones transport, metabolism and biological effects of K2&K5
glucocorticoids and mineralocorticoids. Hypo and
hyper function- Cushing’s syndrome,
aldosteronism, CAH, aderenal cortical
insufficiency, Addison’s disease.
Adrenal medullary hormones- synthesis,
secretion, metabolism, regulation and biological
effects of catecholamines.Phaeochromocytoma.

IV. Gastrointesti Gonadal hormones: Biosynthesis, regulation, K1, K2& 15

nal , transport, metabolism and biological actions of K5
Pancreatic androgens. Hypogonadism and
and Gonadal gynecomastia.Biosynthesis, regulation, transport,
hormones metabolism and biological effects of oestrogen
and progesterone. The menstrual cycle. Pancreatic
hormones- synthesis, regulation, biological effects
and mechanism of action of glucagon,
somatostatin and insulin. Insulin receptor. Brief
account of gastrointestinal hormones.

V. Signal Fundamental concepts and general features of cell K1 & K2 15

transduction signalling. Endocrine, paracrine,
and Neuro autocrinesignaling and juxtacrine signalling.
transmitter Types of receptors. Nuclear and cytosolic
receptors. G-protein-coupled receptors. Second
messengers: c-AMP, cGMP, inositol triphosphate
and Ca 2 +. Receptor tyrosine kinases- insulin
signalling, ras-raf-MAP kinase and JAK-STAT
pathways. Neurotransmitter receptor- Cholingeric
and adrenergic.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
REFERENCE:

Text Books

1. Hadely,M. and Levine,J.E. 2006. Endocrinology, 6 th Edition, Benjamin Cummings.

2. Smith,E. et al., 1983. Principles of Biochemistry, 7 th Edition, McGraw Hill
International Book Co.

Reference Books
1. Guyton,A.C. and Hall,J.E. 2010. Text book of Medical Physiology, 12 th Edition,
Saunders Publishers.
S. Melmed et al., 2015. Williams Text Book of Endocrinology, 13 th Edition, Saun

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L M M L M L L
CO2 H L M M L M L L
CO3 H M M M L M L L
CO4 H L M M L M L L
CO5 H L M M L L L L

H-High; M-Medium; L-Low

 CANCER BIOLOGY

COURSE CODE : 18BCHE02 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : To understand the epidemiology of cancer, mechanism of
oncogenesis and apoptosis, and currently available therapeutic
treatments.

COURSE OUTCOMES (CO)

CO1 To have an understanding , basic knowledge on various cancer growth and
morphology of cancer , terminologies used , types and prevalence of cancer, to
have a further in depth knowledge in the continuing units
CO2 Develop an understanding of how a cancer cell develops into a malignant tumor, the
mechanisms of DNA damage through various agents and how this process is linked
to cellular transformation and cancer risk.
CO3 Understand the common cellular and molecular mechanisms that are deregulated in
cancer cells and the reason for their deregulation. And also the relationship between
diet and cancer, free radicals and antioxidants balance/ role in cancer development.
CO4 To have a better understanding on the impact of apoptosis, its types on
oncogenesis, cancer diagnosis via several different met hods, cytotoxicit y
assays, which will enable the student to be aware on current diagnostic tools
and the principles behind it.

CO5 Having basic knowledge on novel therapeutic approaches available for cancer and its
assessment/ identification by different cancer markers.

SYLLABUS

Unit Unit title Intended Learning chapters Knowled Hours

ge of
domain Instruct
ion
I Introduction Cancer cell-morphology and growth K1,K2 11
characteristics. Types of growth-hyperplasia,
dysplasia, anaplasia and neoplasia. Types and
prevalence of cancer. Nomenclature of neoplasms,
classification based on origin/organ.
II Epidemiology Endocrinology of cancer. Agents causing cancer- K1,K2 11
of cancer radiation, viruses, chemicals. Multistep
carcinogenesis: Initiation, Promotion,
 Progression. Paraneoplastic syndromes.
III Molecular proto oncogenesis, oncogene, oncoproteins, K1, 11
mechanism tumour suppressor genes involved in cancer. Free K2,K4
radicals and antioxidants in cancer. Diet and
cancer. Cell cycle and cancer: Control of the cell
cycle-cyclins and CDKs
IV Apoptosis and Intrinsic and extrinsic pathways-. Mechanism of K1,K2,K 11
cancer apoptosis, signaling pathways. Types and their 3,K4
impact on apoptosis and oncogenesis. Principles
and methods of cancer diagnosis-Biochemical,
genetic, cytotoxic, cell growth and viability tests.
V Cancer therapy Different forms of therapy, chemotherapy, K1, 10
radiation therapy, gene therapy, immune therapy, K2,K3,K
surgical therap y and biologic therapy. Principles 4
of cancer biomarkers and their applications.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES:
Text Books
1. Franks,L.M. and Teich,N.M. 1991. An introduction to Cellular and Molecular
Biology of cancer, 2 nd Edition, Oxford University Press.
2. Vincent,T. et al., 2011. Principles and Practice of Oncology: Primer of the
Molecular Biology of Cancer, 1 st Edition, Lippincott Williams and Wilkins.
3. Weinberg,R.A. 2013. The Biology of Cancer, 2 nd Edition, Garland Science.
4. Hesketh,R. 2013. Introduction to Cancer Biology, Cambridge University Press.

Reference Books
1. McKinnell, R.G. et al., 2006. The Biological Basis of Cancer, 2 nd Edition,
Cambridge University Press.
2. Pelengaris,S. and Khan,M. 2002. The Molecular Biology of Cancer, 2 nd Edition,
Wiley Blackwell.
MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L L M L M L L
CO2 H L M M L M L L
CO3 H L M M L M L L
CO4 H L M M L M L L
CO5 H L L M L M L L

H-High; M-Medium; L-Low

 BIOSTATISTICS

COURSE CODE : 18BCHE03 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : The course emphasizes on various statistical methods and its
significance. The students are expected to understand the
concepts and solve relevant problems pertaining to each topic for
the design of basic research and analysis of research data.

COURSE OUTCOMES (CO)

CO1 This course covers the basic tools for the collection, analysis and
presentation of data in all areas of research.
CO2 To measure the central tendency, variation and correlation analysis
CO3 To compare and emphasis on probability and theoretical distributions
CO4 To analyze sampling distribution, sampling of variables and test of
significance
CO5 To study the Analysis of variation and design of experiment

SYLLABUS

Unit Unit title Intended Learning chapters Knowled Hours

ge of
domain Instruct
ion
I Introduction Organizing a statistical survey, Planning and K1.K2. 13
executing the survey. Source of data - Primary K3
and secondary data, collection, observation,
interview, enquiry forms, questionnaire schedule
and check list. Classification and tabulation of
data. Diagrammatic and graphic presentation of
data.
II Measures of Measures of central tendency - arithmetic mean, K1.K2. 14
central median, mode, quartiles, deciles and percentiles. K3, K4
tendency and Measures of variation - range, quartile deviation,
correlation mean deviation, standard deviation, Coefficient of
analysis variation. Correlation analysis - Scatter diagram,
Karl's Pearson's coefficient of correlation and
Spearman's rank method. Regression analysis.
III Probability and Probability- Definition, concepts, theorems (proof K1.K2. 14
theoretical of the theorems not necessary) and calculations of K3.K4
distributions probability. Theoretical distributions – Binomial,
 Poisson and normal distribution-Simple problems.
IV Sampling Sampling distribution and test of significance – K1.K2. 16
distribution Concepts of sampling, Testing of hypothesis, K3, K4
and test of errors in hypothesis testing, standard error and
significance sampling distribution, sampling of variables (large
samples and small samples.). Student's "t"
distribution and its applications. Chi-square test
and goodness of fit.
V Analysis of Analysis of variance - one way and two way K1.K2. 15
variance classification. Duncan's Multiple Range test. K3, K4
Mann Whittneys test-significance. Design of
experiment-Completely randomised block design,
Randomised block design.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
REFERENCES:
Text Books
1. Gupta,S.P. 2011. Statistical Methods, 4 th Edition, Sultan Chand & Son Publishers.
2. Zar,J.H. 2010. Biostatistical Analysis, 5 th Edition, Pearson Education..

Reference Books
th
1. Daniel,W.W. 2008. Biostatistics - A Foundation for Analysis in Health Sciences, 9
Edition, John Wiley and Sons, Inc., 1999.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H L L L M L L L
CO2 H L M L M L L L
CO3 H L M L M M L L
CO4 H L M L M M L L
CO5 H L M L M L L L
H-High; M-Medium; L-Low
 MICROBIOLOGY

COURSE CODE : 18BCHE04 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : Understand the basic information about microbiology, virology,
medical, food and industrial microbiology

COURSE OUTCOMES (CO)

CO1 It provides the basic concepts of morphology, cytology and classification of
microbes.
CO2 It helps to understand the molecula mechanism behind viral infections.
CO3 Understanding of pathogenesis of microbial diseases affecting humans.
CO4 To educate the beneficiary role of microorganism.
CO5 To understand and appreciate the different industrial applications of microbes.

SYLLABUS

Unit Unit title Intended Learning chapters Knowled Hours

ge of
domain Instruct
ion
I Morphology, Bacterial nomenclature and classification; K1.K2. 13
cytology and prokaryotic organism on overview, morphology K3
classification and ultra structure of bacteria, shapes and
microbes arrangement of bacteria, morphology types;
archeabacteria, gram positive and gram negative
and subacteria structure and function of flagella,
cilia and endospore. Structure and classification
of algae and reproduction. Structure and
classification of fungal cell, hypae, spores,
Protozoa. Light microscopy- bright field, dark
field, phase contrast, fluorescent and polarization
microscope, electron microscopy, TEM & SEM.

II Virology Nomenclature – classification and taxonomy of K1.K2. 14

viruses; host, nucleic acids and structure. K3
Bacterial viruses; ØX 174; T4; M13A, life cycle
(Lysogenic and Lytic). RNA phages plant viruses;
effects of viruses on plants, RNA viruses, TMV,
satellite viruses, bromo mosaic virus. Animal
viruses; classification and structure of animal and
human viruses. RNA viruses; Herpes virus, RNA
tumor virus-retro virus, DNA virus – vaccinia
 virus, SV40 adeno viruses. Viroids.
III Medical Normal microbial flora of human body – K1.K2. 14
microbiology (respiratory tract, skin, GIT, Infection – sources) K3
mode of transmission (exogenous and
endogenous).Mechanism of bacterial
pathogenesis. Medically significant bacteria
Staphylococcus aureus, Streptococci, pathogenic,
enterobacteriaceae, Vibrio, Corny bacterium,
pseudomonas, Mycobacterium tuberculosis,
Helicobacter pylori. Pathogenesis of parasitic
disease, blood and tissue protozoa, nematodes,
arthropods, influenza viruses, measles, chicken
pox, hepatitis , dengue fever, Mechanism of
fungal pathogenesis, superficial and cutaneous
mycoses, systemic mycoses, opportunistic
mycoses.
IV Food Food as substrate for the microorganisms. General K1.K2. 16
microbiology principles and types of microbes in spoilage of K3
and diary foods, different methods of preservation.
microbiology Microbes in food: mold, yeast, bacteria. Food
borne diseases: Staphylococcus, Clostridium,
E.Coli, Salmonella, mycotoxin, Protozoan. Viral
food borne disease. Microflora of milk- sources of
contamination-intoxication-pasteurization-
sterilization-fermented diary products-yogurt,
kafir, kumiss, cheese production. Food hygiene
and control-food sanitation in food manufacture.
V Industrial Industrial microbiology; an introduction to K1.K2. 15
Microbiology fermentation process- components parts of K3
fermentation process. Industrially important
organisms- upstream processing, media for
industrial fermentation, formulation and
sterilization. Aerobiology – droplet nucleus –
aerosols – transmission of microbes –assessments
of air quality and diseases. Soil Microbiology :
Soil microbes, Soil Pollution – Micro flora of
various soils – Biofertilizers Geomicrobiology –
Biochemical cycles of Carbon, Nitrogen,
Phosphorus, Sulphur and Iron cycles.
Biobleaching & Biomining – Petroleum
degradation- Xenobiodegradation.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

Text Books
1. Prescott, M.L., Harley, P.J. and Klein, A.D. 2004. Microbiology, 6 th Edition,
McGraw-Hill Science.
2. Pelczar, J.M. et al., 2001. Microbiology, 5 th Edition, Tata-McGraw Hill
Publications.
3. Ananthanarayanan R and Jayaram Paniker, C.K. 2009. Textbook of
Microbiology, 8 th Edition, Universities Press.

REFERENCES
Reference Books
1. Medical Microbiology. Jawetz, Melinickand Adelberg’s, Twenty Second
Edition,
McGraw Hill Medical Publication division, 2001.
2. Pommerville, J.C. Alcamo, I.E. . 2012. Alcamo's Fundamentals of Microbiology,
Jones & Bartlett Publishers.

3. Cruegar,W. and Cruegar. A., Biotechnology : A Textbook of Industrial

Microbiology Second Edition, Panima Publishing Corporation, Bangalore,
2004.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 M M L L L L M L
CO2 M M L L L L M L
CO3 M M L L L L M L
CO4 M M L L L L M L
CO5 M M L L L L M L
H-High; M-Medium; L-Low
 NUTRITIONAL BIOCHEMISTRY

COURSE CODE : 18BCHE05 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : To provide an understanding of biochemistry and explores the
biochemical activity in the human body of nutrients and food
constituents.

COURSE OUTCOMES (CO)

CO1 The students will gain theoretical information on energy metabolism and
carbohydrates
CO2 To study the basics of protein and lipid biomolecules
CO3 To understand the importance of electrolytes, minerals and vitamins in human
body
CO4 To study and analyze the importance of nutraceuticals and its importance in
phytotherapeutics
CO5 To study the clinical relevance of nutritional biochemistry.

SYLLABUS

Unit Unit title Intended Learning chapters Knowled Hours

ge of
domain Instruct
ion
I Introduction to Basic concepts : Composition of human body. K1.K2. 13
energy Energy metabolism - Energy content of foods- K3
metabolism and direct and indirect methods. BMR and SDA -
carbohydrates methods of measurement of energy expenditure.
Thermogenic effects of foods. Recommended
dietary allowances, Food Pyramid. Carbohydrates
: Dietary requirements and sources of available
and unavailable carbohydrates. Physico-chemical
properties and physiological actions of
unavailable carbohydrates (dietary fiber).

II Proteins and Proteins : protein reserves of human body. K1.K2. 14

Lipids Nitrogen balance studies and factors influencing K3
nitrogen balance. Essential amino acids for man
and concept of protein quality. Cereal proteins
 and their limiting amino acids. Protein
requirement at different stages of development.
Protein deficiency disorders. Lipids : Major
classes of dietary lipids. Properties and
composition of plasma lipo - proteins. Dietary
needs of lipids. Essential fatty acids and their
physiological functions.

III Electrolytes, Electrolytes and water balance : Electrolyte K1.K2. 14

minerals and concentration of body fluids. Acids base K3
vitamins regulation by the human body. Concepts of
metabolic and respiratory acidosis and alkalosis.
Minerals : Nutritional significance of dietary
calcium, phosphorus, magnesium, iron, iodine,
zinc and copper. Vitamins: Dietary sources,
biochemical functions and specific deficiency
diseases associated with fat and water – soluble
vitamins. Hypervitaminosis symptoms of fat –
soluble vitamins.

IV Nutraceuticals Nutraceuticals: significance in human health . K1.K2. 16

and Antioxidants : antioxidant enzymes- mode of K3,K4
phytotherapeut action, non-enzymic antioxidants- mechanism of
cs action, Phytotherapeutics: phenolic compounds,
flavonoids, lycopene, carotenoids, anthocyanins.
Vitamin A,E,B and C. Dietary metabolism and
health Over view and risks of dietary
supplements. Nutrition for infants, children,
teenagers, pregnancy and lactation and ageing.

V Applied Eating disorders- Obesity, anorexia nervosa and K1.K2. 15

nutrition bulimia nervosa, total parenteral nutrition (TPN), K3,K4
sports nutrition, poverty and nutrition, Food
allergies - immune reactions. Applied nutrition:
Diet- nutrition, and lifestyle-related chronic non-
communicable diseases (NCDS) - cardiovascular
diseases, diabetes mellitus, cancer, diseases of
kidney, nutrition and HIV/AIDS, food and
nutrition security in developing countries.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)
REFERENCES
Text Books
1. Bamji,M.S.et al., 2009. Text book of Human Nutrition, 3 rd Edition, Oxford and
IBH Publishers.
2. Insel, P. et al. 2013. Discovering Nutrition, 4 th Edition, Jones and Bartlett
Publishers.
3. Swaminthan, M.S. 1986. 2007. Handbook of Food and Nutrition, 5 th Edition.
The Bangalore Printing and Publishing Company.

Reference Books
1. Srilakshmi,B. 2006. Nutrition Science, 2 nd Edition, New Age International
Publishers.
2. Weighley, E.S. 1997. Robinson’s Basic Nutrition and Diet Therapy, 8 th Edition,
Macmillan Publishers.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 M L L M L M L L
CO2 M L L M L M L L
CO3 M L L M L M L L
CO4 M L L M L M L L
CO5 M L L M L M L L
H-High; M-Medium; L-Low
 BIOTECHNOLOGY

COURSE CODE : 18BCHE06 Hours L T P C

MARKS : 100 3 1 0 4
COURSE
OBJECTIVES : The objective of this course is to have a basic foundation on
bioprocess, industrial, animal, medical and environmental
Biotechnology.

COURSE OUTCOMES (CO)

CO1 Understand the basic principles involved in bioprocess technology including
fermentation, its types, downstream processing, sterilization of culture media will
form a good foundation for advanced learning.
CO2 Understand the basics in microbiology including isolation of a strain as well as
identification, production of microbial metabolites, antibiotics through microbial
methods, the need for genetic improvements and the process of carrying it out, Single
cell protein and its significance.
CO3 Understand the basics in histopathology performance, culture media used for animal
cell culture systems – primary, secondary cell culture, its characterization,
cytotoxicity assays, gene cloning will help the students to have a wider knowledge in
the latest technology.
CO4 Have a basic knowledge on the use of DNA in diagnosing infections via DNA finger
printing, pharmaceutical products developed by RDNA technology for certain
specific diseases, Vaccine production from plants , studying its types etc will give a
strong basic foundation to attain their focused specialization .
CO5 Having basic knowledge in the pollution monitoring, pollutant degradation via
biotechnological methods – bioremediation available for solid waste management ,
soil pollution reduction will help the students to maintain an eco friendly
environment which will protect the future generations on the whole as well as
reduced global warming.

SYLLABUS
Unit Unit title Intended Learning chapters Knowledg Hours
e domain of
Instructi
on
I Bioprocess Bioreactors: types, operation of conventional K1,K2.K 11
technology bioreactor, solid substrate fermentation, *Media 3
for industrial fermentation, sterilization of culture
media and gases.Batch culture, Fedbatch culture,
and continuous culture Downstream processing:
 solid-liquid separation, release of intracellular
products, concentration, purification and
formulation
II Industrial Isolation of microorganism, microbial metabolic K1,K2,K 11
Biotechnology products - primary and secondary metabolites, 3
genetic improvement of strains. Metabolite
production : Organic solvent – alcohol, organic
acids – citric acid and lactic acid, antibiotics –
penicillin and streptomycin, vitamins – riboflavin
and ascorbic acid.Single cell protein
III Animal Animal cell culture: fundamentals and K1, 11
Biotechnology applications. Organ and tissue slice techniques. K2,K3
Culture media for animal cells, cultured cells –
Biology and characterization, primary culture and
cell lines, cell viability and cytotoxicity, cell
transformation and cell cloning
IV Medical DNA in disease diagnosis : DNA probes, DNA in K1,K2,K 11
Biotechnology diagnosis of infectious diseases, genetic diseases, 3
DNA fingerprinting. Pharmaceutical products of
DNA technology : Human protein replacement,
therapeutic agents for human diseases.
Recombinant vaccines : subunit vaccines, DNA
vaccines, attenuated recombinant vaccines, plants
as edible subunit vaccines.
V Environmental Environmental pollution : Types of pollution, K1, 10
Biotechnology pollution monitoring, biotechnological methods K2,K3
for management of pollution. Biodegradation :
xenobiotic compounds. Bioremediation: Types of
bioremediation, types of reactions in
bioremediation, genetic engineering for efficient
bioremediation, bioremediation of contaminated
soil and waste land.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES:
Text Books
1. Satyanarayana,U. 2005.. Biotechnology, 1 st Edition, Books & Allied Ltd.
2. Clark,D.P.and Pazdernik,N.J. 2009. Biotechnology: Applying the genetic
revolution, Elsevier.
 3. Singh,B. and Gautam,S.K. 2013. Textbook of Animal Biotechnology, The Energy
and Resources Institute, TERI.
Reference Books

1. Cruger,W. and Cruger,A. 2000. Biotechnology: A text book of Industrial

Microbiology, 2 nd Edition, Sinauer Associates Inc.
2. Stanbury,P. and Whitaker,A. 1984. Principles of Fermentation Technology, 1 st
Edition, Pergamon Press.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 M L M M L M L L
CO2 M L M M L M L L
CO3 M L M M L M L L
CO4 M L M M L M L L
CO5 M L M M L M L L
H-High; M-Medium; L-Low
SUPPORTIVE COURSES FOR OTHER
DEPARTMENTS
 TOOLS AND TECHNIQUES IN BIOSCIENCE

COURSE CODE : 18BCHS01 Hours L T P C

MARKS : 100 3 0 0 3
COURSE
OBJECTIVES : To understand the principles, instrumentation and applications of
major analytical techniques used in biosciences.

COURSE OUTCOMES (CO)

CO1 To understand the techniques in cell fractionation. To understand the techniques and
applications of radioisotopes in biology.
CO2 To understand the principles and applications of centrifugation and microscopy
CO3 To understand the principles and applications of chromatography.
CO4 To understand the principles and applications of electrophoretic techniques.
CO5 To understand the principles and applications of spectroscopy.

SYLLABUS

Unit Unit title Intended Learning chapters Knowledge Hours

domain of
Instruct
ion
I K1,K2,K3 13
Cell- Cell lysis, homogenization extraction, salting
fractionation in, salting out, dialysis and ultra-filtration.
technique, Concepts of half-life, decay constant, detection
Radioisotopes and quantitation- GM counter and solid and
in Biology liquid scintillation counter. Specific activity,
autoradiography and their applications.
Application of radioactivity.
II Centrifugation, Svedberg’s constant, sedimentation velocity K1,K2,K3 13
Microscopy and sedimentation equilibrium. Differential and
density gradient centrifugation, centrifugal
elutriation, construction of preparative and
analytical ultracentrifuge. Principles and
applications of light phase contrast,
fluorescence, scanning and transmission
electron microscopy
III Chromatographi Principles and applications of paper, TLC, K1, K2, K3 13
c techniques adsorption, ion exchange, gel filtration,
affinity, GLC, chromate focusing, HPLC and
 FPLC.
IV Electrophoretic Polyacrylamide gel electrophoresis, SDS- K1, K2, K3 13
techniques PAGE, 2D- electrophoresis, agarose gel
electrophoresis, isoelectric focusing, pulsed
field electrophoresis, high voltage
electrophoresis, capillary electrophoresis,
isotachophoresis.
V Spectroscopic Principles of colorimeter, spectrophotometer, K1, K2,K3 13
techniques fluorimeter. Beer-Lambert’s Law and its
limitation. Extinction coefficient, Atomic
absorption spectroscopy UV-Visible,
Spectrofluorometry, Flame photometry,
Nephlometry, Turbidometry.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES
Text Books
1. Wilson,K. and Walker,J. 2005. Principles and Techniques of Practical
th
Biochemistry, 6 Edition , Cambridge University. Press .
2. Upadhyay,A. Upadhyay,K. and Nath,N. 2009. Biophysical Chemistry: Principles and
Techniques, Third Edition, Himalaya Publishing. 11 th Edition
Reference Books
1. Sharma,B.K. 1981. Instrumental Methods of Chemical analysis, 5 th Edition Goel
Publications.
2. Homie,D.J. and Peck,H. Analytical Biochemistry, Third Edition, Longman

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M M L L M L
CO2 H M M M L L M L
CO3 H M M M L L M L
CO4 H M M M L L M L
CO5 H M M M L L M L
H-High; M-Medium; L-Low
 MEDICAL LAB TECHNOLOGY
COURSE CODE : 18BCHS01 Hours L T P C
MARKS : 100 3 0 0 3
COURSE
OBJECTIVES : This syllabus has been formulated to impart basic knowledge of
biochemistry, analytical techniques and to perform clinical
laboratory tests accurately and efficiently.

COURSE OUTCOMES (CO)

CO1 To gain knowledge in the general laboratory instruments and equipment and to
know about the specimen processing for biochemical analysis.
CO2 To understand the principles and applications in the analytical techniques.
CO3 To understand the principles and applications of biochemical tests.
CO4 To understand the principles and applications of automation of the analytical
processes in clinical laboratory.
CO5 To understand the laboratory information systems.

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I General approach Safety in the laboratory. General laboratory K1,K2,K3 13
to medical instruments and equipments . Basic Chemistry and
laboratory laboratory calculations . Specimen processing for
sciences Biochemical analyses - Blood, urine, cerebrospinal
fluid, synovial fluid.
II Principles of Basic concepts in analytical chemistry, Colorimetry, K1,K2,K3 12
Analytical Spectrophotometry, titrimetry, flame photometry,
techniques chromatography, electrophoresis. Immunochemistry -
ELISA, RIA, CLIA, PCR techniques, flow cytometry
and biochips.
III Clinical Biochemical tests - glucose, protein, albumin, urea, K1,K2,K3 15
Chemistry creatinine, uric acid, bilirubin and cholesterol. ,K4
Enzymes - SGOT, SGPT, ALP, ACP, LDH,
creatinine kinase, lipase, amylase, choline esterase.
Hormones - Insulin, T3, T4, TSH, cortisol, FSH,
progesterone and estrogen. Electrolytes and blood
gases Biochemical profile test: Liver function test,
renal function test, gastric function test, pancreatic
function test and endocrine function test.
IV Automation in Basic concepts, Automation of the analytical K1,K2,K3 13
Clinical processes, Steps of automation in biochemical
laboratory analysis, Computers in the clinical laboratory, Types
of automated analysers, Commonly used analysers of
biochemical laboratories. Statistical procedures –
 Arithmetic mean, Median, standard deviation,
coefficient of correlation, t test and ANOVA.
V Laboratory Clinical laboratory informatics - Computer systems, K1,K2,K3 13
management Laboratory information systems, Laboratory ,K4
Management – Basic concepts, financial management
. Quality management – Fundamentals, Total quality
management of clinical laboratory.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES

Text Books
1. Mukherjee,K.L. 1988. Medical Laboratory Technology – A procedure manual for
routine diagnostic tests, Vol I , II, III. Tata McGraw Hill Publishing Company
Limited.
2. Burtis,C.A. and Ashwood,E.R. 2007. Teitz Textbook Clinical Chemistry., Third
Edition, W.B.Saunders Company.
3. Varley,S. 1988. Practical Clinical Biochemistry, Gowenlock et al., Sixth Edition,
CBS Publishers & Distributors. 1988

Reference Books
1. Henry,J.B. 1988. Clinical Diagnosis and Management by Laboratory Methods.,
17 th Edition, W.B.Saunders Company.
2. Chatterjee,M.N. and Shinde,R. Text book of Medical Biochemistry, 5th Edition,
Jaypee Brothers Medical Publishers, 2002.
3. Devlin,T.M. 1998. Text book of Biochemistry with Clinical Correlation, 4 th
Edition, John Wiley and Sons.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M M L L M L
CO2 H M M M L L M L
CO3 H M M M L L M L
CO4 H M M M L L M L
CO5 H M M M L L M L
H-High; M-Medium; L-Low
 CLINICAL DIAGNOSIS IN HEALTH AND DISEASES
COURSE CODE : 18BCHS03 Hours L T P C
MARKS : 100 3 0 0 3
COURSE
OBJECTIVES : The aim of the course is to understand the diagnostic procedures
adopted in various disease conditions and its management.

COURSE OUTCOMES (CO)

CO1 To know about general health, syndrome and common diseases that affects mankind
CO2 To understand the importance of liver and kidney function test
CO3 To understand the basics and importance of heart, lung and brain test
CO4 To know the basic mechanisms of communicable diseases
CO5 To imbibe and understand the mechanism of non- communicable diseases and
their clinical significance

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I Introduction General health, syndrome and common diseases – K1,K2,K3 13
communicable and non-communicable diseases.
Samples for analysis: Blood, urine, pleural fluid,
synovial fluid, cerebrospinal fluid and tissues and
histology. General check up: Blood group, Hb,
height and weight, waist to hip ratio, electro
cardio gram, X-ray, abdomen scan and
appearance of scars, urine analysis – routine
analysis (protein, sugar, pigments and cells).
II Liver and kidney Detection of metabolites and its importance. K1,K2,K3 12
function test Tests for liver function: Enzyme assay (SGOT,
SGPT, Alkaline phosphatase, GGT), Total
protein, albumin /globulin ratio and their
significance. Test for kidney function: Urea and
creatinine estimation and their significance.
III Heart, lung and Test for heart function: Blood pressure (cystolic K1,K2,K3 15
brain test and diastolic), lipid profile (cholesterol,
triglycerides, HDL, LDL estimation) and their
importance. Test for lung function: Chest X-ray,
Spirometry. Test for Brain function: EEG, MRI,
CT. Test for Surgery: Bleeding time, clotting
 time. Special test: X-ray, CT, MRI, Doppler,
TMT, angioplasty.

IV Infections Infection: Bacterial, viral, fungal and protozoans. K1,K2,K3 13

Blood: Total cell count, differential count,
erythrocyte sedimentation rate. Infectious
diseases: Tuberculosis, Leprosy, Malaria,
Hepatitis, Cholera, Dengue, HIV, Chikun gunya
and H1N1. TORCH – Panel (infertility profile),
Infection in pregnancy, Koch postulations –
Microscopic examination of body fluids, ELISA
and PCR tests.

V Non Non communicable diseases: Diabetes: Blood K1,K2,K3 13

communicable sugar, urine sugar, glucose tolerance test,
diseases HbA1c. Hyper tension: Lipid profile, electrolyte
(sodium, potassium, chloride and biocarbonate)
investigation. Cancer markers: ELISA.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES

Text Books
1. Burtis,C. and Bruns,D. 2007. Teitz Fundamentals of Clinical chemistry
Chemistry, 3 rd Edition W.B.Saunders Company.
2. Devlin,T.M. 1998. Text book of Biochemistry with Clinical Correlation,
4 th Edition.
3. Varley,H. 1980.Practical Clinical Biochemistry, Volume I and II, 5 th Edition, CBS
Publishers.
Reference Books
1. Mayne,P.D. 1994. Clinical Chemistry in Diagnosis and Treatment, 6 th Edition,
Hodder Arnold Publication.
2. Marshall,W.J. and Bangeit, S.K. 1995. Clinical Biochemistry - Metabolic concepts
and Clinical aspects, Churchill Livingstone.
3. Guyton,A.C. and Hall,J.E. 2010. Text Book of Medical Physiology, 12 th Edition,
Saunders.
MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M M L L M L
CO2 H M M M L L M L
CO3 H M M M L L M L
CO4 H M M M L L M L
CO5 H M M M L L M L
H-High; M-Medium; L-Low
 INTRODUCTION TO BIOCHEMISTRY
COURSE CODE : 18BCHS04 Hours L T P C
MARKS : 100 3 0 0 3
COURSE
OBJECTIVES : This course is an introduction to biochemistry and covers the
structure and functions of biological molecules.

COURSE OUTCOMES (CO)

CO1 Understand the basics involved in the structure of carbohydrates like
anomerism,stereoisomerism, epimer formation and their types, chemical properties,
and functions.
CO2 Understand the basics in the structure of lipids, classifications like simple and
complex lipid including lipopotein and lipo polysaccharides and teir biological
functions.
CO3 Understand the basic structure- types, classification, properties-coagulation,
denaturation, function of protein, amino acids and its sequencing.
CO4 Have a basic knowledge on the structure of DNA, experiments that proved it as a
genetic material, as well as to know their properties, functions in biology.
CO5 Know about the structure, types of vitamins in biological reactions, and its
relationship with disease, daily requirement.

SYLLABUS

Unit Unit title Intended Learning chapters Knowledg Hours

e domain of
Instructi
on
I Carbohydrates Classification-monosaccharides, disaccharides, K1,K2,K3 13
polysaccharides basic chemical structure, aldoses
and ketoses, cyclic structure of mo
nosaccharides, steroisomerism, anomers and
epimers. Sugar derivatives, deoxy sugars, amino
sugars, and sugar acids. General reaction and
properties. Structure and biological functions of
homo- and heteropolysaccharides.
II Lipids Classification, structure, properties and functions K1,K2,K3 12
of fatty acids, essential fatty acids, fats,
phospholipids, sphingolipids, cerebrocides,
steroids, bile acids, prostaglandins, lipoamino
acids, lipoproteins, proteolipids,
phosphatidopeptides, lipopolysaccharides.
III Proteins Classification, structure and properties of amino K1,K2,K3 15
acids, biologically active peptides, classification
and properties of proteins, sequencing of
proteins, conformation and structure of proteins -
primary, secondary, tertiary and quaternary
 structure, coagulation and denaturation of
proteins.
IV Nucleic acids Nucleic acids as genetic information carriers, K1,K2,K3 13
experimental evidence e.g., genetic
transformation, Hershey-Chase experiments,
action spectrum, etc. Structure and function of
nucleotides. Primary, secondary and tertiary
structure of nucleic acids, DNA forms and
conformations, Denaturation of DNA.
V Vitamins Structure, biochemical functions, deficiency K1,K2,K3 13
diseases, daily requirements of water soluble and
fat soluble vitamins and their coenzyme activity.

Program specific attributes

Knowledge and understanding level (K1 and K2)
Application level (K3)
Analytical level (K4)
Evaluation capability level (K5)
Scientific or synthesis level (K6)

REFERENCES

Text Books
1. Nelson,D.L and Cox,M.M.2013. Lehninger Principles of Biochemistry, 6 th
Edition, W.H. Freeman
2. Garrett,R. and Grisham,C. 2010. Biochemistry, 4 th Edition, Saunders College
Publishing
Reference Books
1. Berg,J.M. et al. 2012. Biochemistry, 7 th Edition, W. H. Freeman & Company,
2012.
2. Voet,D. et al., 2012. Fundamentals of Biochemistry: Life at the Molecular level,
4 th Edition, John Wiley and Sons.

MAPPING

PO
CO PO1 PO2 PO3 PO4 PO5 PO6 PO7 PO8

CO1 H M M M L L M L
CO2 H M M M L L M L
CO3 H M M M L L M L
CO4 H M M M L L M L
CO5 H M M M L L M L
H-High; M-Medium; L-Low