BIOCHEMISTRY

and

BIOCHEMISTRY EXPERIMENT

 

 

Course Number:

Prerequisites: Inorganic Chemistry, Organic Chemistry, Biology

Credits for BIOCHEMISTRY (periods per week ): 4.5(4.5)

Credits for  BIOCHEMISTRY EXPERIMENT (periods per week):1.5(8)

Year: 1st year ,1^st semester

 

COURSE DESCRIPTION:

How does a doctor diagnosis a patent who may have had a heart attack? What is the background to the screening of newborn infants for inborn errors of metabolism? Medical biochemistry will emphasis on above topics and other related medical problems throughout whole course. The course will cover the following topics: 1. Structure, function and interrelationship of biomolecules and consequences of deviation from normal; 2. Basic and clinical aspects of enzymology and regulation of enzymatic activity; 3. Integration of the various aspects of metabolism, and their regulatory pathways; 4. Basic concepts about vitamins; 5. Basic concepts about hormones; 6. Hematic biochemistry; 7.Molecular mechanisms of gene expression and regulation, the principles of genetic engineering and their application in medicine.

 

OBJECTIVES:

Knowledge

At the end of the course, the student should be able to: demonstrate his knowledge and understanding on the:

1. Molecular and functional organization of a cell, and sub- cellular components;

2. Structure, function and interrelationship of biomolecules and consequences of deviation from normal;

3. Basic and clinical aspects of enzymology and regulation of enzymatic activity;

4. Digestion and assimilation of nutrients and consequences of malnutrition;

5. Integration of the various aspects of metabolism, and their regulatory pathways;

6. Biochemical basis of inherited disorders and their associated sequelae;

7. Mechanisms involved in maintenance of body fluid and pH homeostasis;

8. Molecular mechanisms of gene expression and regulation, the principles of genetic engineering and their application in medicine;

9. Molecular concepts of body defence and their application in medicine;

10. Biochemical basis of environmental health hazards; and biochemical basis of cancer and carcinogenesis, principles of metabolism, and detoxication of xenobiotics.

11. Principles of various conventional and specialized laboratory investigations and instrumentation, analysis and interpretation of a given data; the ability to suggest experiments to support theoretical concepts and clinical diagnosis.

Skills

At the end of the course, the student should be able to

1. make use of conventional techniques/ instruments to perform biochemical analysis relevant to clinical screening and diagnosis

2. analyze and interpret investigative data

3. demonstrate the skills of solving clinical problems and decision making.

COURSE CONTENT:

Lectures

I. Biomolecules （10 periodes）

(a) Classification and cellular function of carbohydrates, lipids, protein and nucleic acids and their structures.

(b)Structural organization and structure-function relationships of proteins..

(c)Cell membrane structure and functions .

II. Enzymes （5 periodes）

(a) Nomenclature, classification,

(b) Kinetics, mechanism of enzymatic catalysis.

(c) Factors influencing enzymatic catalyses, enzyme activators and inhibitors.

(d) Regulation of enzyme activity,

(e) Clinical enzymology, isoenzymes.

III. Metabolic pathways, their regulation and metabolic interrelationships（27 periodes）

Metabolism: general concepts and characteristics of metabolic pathways.

Carbohydrate metabolism

(a) Digestion and absorption of dietary carbohydrates

(b) Pathways of glucose metabolism: glycolysis

(c) Pentose phosphate shunt

(d) Gluconeogenesis

(e) Glycogenolysis, glycogenesis

(f) Galactose and fructose metabolism

(g) Glycogen storage disease

(h) Inborn errors of glucose metabolism

(i) Regulation of glucose metabolism.

Protein turnover and amino acid metabolism

(a) Digestion and absorption of dietary protein

(b) General reactions, transamination, its metabolic and diagnostic significance

(c) Disposal of amino acid nitrogen and detoxication of urea

(d) Metabolic fate of amino acid carbon skeleton

(e) Sulphur containing amino acids

(f) In born errors of branched chain and aromatic amino acids

(g) Important amino acid derivatives.

Lipid metabolism

(a) Digestion and absorption of dietary fats.

(b) Biosynthesis and degradation of fatty acids, phospolipids and triacylglycerols

(c) Biosynthesis of cholesterol, chemistry and metabolism of lipoproteins.

(d) Hyperlipoproteinemias

(e) Lipid storage disease.

(f) Ketone bodies: their synthesis, utilization and conditions leading to ketoacidosis, prostaglandin.

TCA cycle and biological oxidation, prostanoids.

Regulation of the metabolic pathways

(a) Carbohydrate, lipid and amino acid metabolism

(b) Interlinks between these pathways.

(c) Organ interrelationships in metabolism,

(d) Blood glucose regulation, and its impairment in diabetes mellitus.

(e) Metabolic adaptation in the fed state, fasting and prolonged starvation.

(f) Metabolic derangements and adaptations in diabetes mellitus.

IV. Hormones （3 periodes）

(a) Molecular basis of hormonal action, signal transduction mechanisms.

(b) Chemistry, functions and mechanism of action of hormones of the pituitary, thyroid, parathyroid, adrenals, panaceas, and gonads.

(c) The functions and mechanism of action.of steroid hormones

(d) Hormonal interplay in the regulation of metabolism.

V. Fat soluble and water soluble vitamins （1.5 periodes）

VI. Hematic Biochemistry （3 periodes）

(a) Regulation of blood pH, acidosis, alkalosis,

(b) Heme synthesis.

(c) (e) Plasma proteins, their functions and clinical significance.

VII. Molecular Biology （22.5 periodes）

(a) DNA Replication,

(b) DNA Transcription

(c) Post-transcriptional processing.

(d) Translation of genetic code

(e) Regulation of gene expression and protein synthesis inhibitors of protein synthesis.

(f) DNA repair mechanisms and related disorders

(g) Applied aspects of purine and pyrimidine metabolism

(h) Genetic Engineering: Recombinant DNA technology

(i) DNA and diagnostics

(j) Telomers, telomerases

 

Practicals

The laboratory-based content is designed to complement the lectures, 8 periods for each experiment

Experiment 1  protein extraction from animal liver and quantitation by various methods

Experiment 2  DNA extraction from eukaryotic cell and quantitation

Experiment 3  protein molecular weight determination by SDS PAGE

Experiment 4  enzymatic kinetics

Experiment 5  chromatographic techniques

Experiment 6  botanic agglutinin: separation and activity determination

 

 

STRUCTURE:

The course comprises 72 periods of lectures and 48 periods of practicals.

One weekly 8 periods practical session will be held.

Assignment will be given at the middle of semester. The final examination (2 hr) for lecture will contain all the contents given in the course.

 

EVALUATION:

Students’ performance in Biochemistry will be evaluated on the basis of attendance at lectures (5%),   assignment (20%) and scores on the final examination (75%).

Students’ performance in Biochemical Experiment will be evaluated on the basis of attendance at practicals (30%), practical reports (70%).

RECOMMENDED TEXTBOOK:

.Biochemistry, Ed by Pamela Champe et al, Williams & Wilkins

SUPPLEMENTARY READING:

1. Biochemistry Ed. Lubert Stryer. W.H. Freeman and Company, New York.

2. Principles of Biochemistry. Ed. Lehinger, Nelson and Cox. CBS Publishers and distributors.

3. Textbook of Biochemistry with Clinical Correlations. Ed. Thomas M. Devlin, Wiley-Liss Publishers..

TEACHING TEAM:

Faculty:

Prof. Xu Lihong

Tel: 88208265

Email: xulihong@zju.edu.cn

Rm 601, Block C, Research Building, School of Medicine, Zijingang Campus

 

Prof. Zhan Jinbiao

Tel: 88208273

Email: jzhan2K@zju.edu.cn

Rm 602, Block C, Research Building, School of Medicine, Zijingang Campus

 

Mr. Chen Yonggang

Email: chenyonggang@zju.edu.cn

 

Dr. Liu Huigang

Email: liuhuigang@hkucc.hku.hk