The curriculum outline of biochemistry Total period 180 (Theory 113, Practice 45, Individual sdudy 22.

) Chapter Chapter 1 Contents Introduction, Structures and Functions of Proteins Total period 12 7 5 Theoy

Chapter 2 Chapter 3 Chapter 4 Chapter 5 Chapter 6 Chapter7 Chapter8 Chapter 9 Chapter 10 Chapter 11 Chapter 12 Chapter 13 Chapter 14

Structures and Functions of Nucleic Acids Enzymes Vitamins Carbohydrates Metabolisms Biological Oxidation Metabolism of Lipids Catabolism of Proteins Nucleotides Metabolism Biosynthesis of DNA Synthesis of RNA Biosynthesis of Protein Regulation of Gene Expression Gene Recombinant & Gene Ingeneering

1 4 1 1 4 17 7 17 12 6 8 14 11 9 10

8 6 4 10 7 10 10 6 6 7 6 7 8

5 5

5 5

5 5

Chapter 15 Chapter 16

Blood Biochemistry Liver Biochemistry

12 13

5 6

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Intruduction to Biochemistry

Biochemistry is the study of life on the molecular level.Therefore, biochemistry, as the name implies, is the chemistry of life. Life, at its most basic level, is a biochemical phenomenon including two basic characteristics: selfrefresh (metabolism), and self-replication and self-assembly (expression and transmission of genetic information). The 21th century is an era of life science. Lots of wonders are being created, and explosive information is being provided at an unprecedented speed. Biochemistry is a window opening to the world of life science. Thus, the knowledge of biochemistry which involves the study of chemical molecules and reactions in living organisms, and the elucidations of the nature of live phenomenon on the molecular level, is essential to medical students, as well as to the students of other related disciplines. As is known to all, when biochemistry is taught in English, it will be double-beneficial to the chinese students and the students abroad, for they get trained in their professional language while learning biochemical knowledge. This is not only significant to students who want to expand their knowledge from other sources written in English, but also helpful to the students who are going to pursue their scientific career in the future. There are four parts in this program, and totally 16 chapters: the structures and functions of biomolecules ( Part I); the metabolism of substrates and their regulations (Part II); expression and transmission of genetic information, Gene Recombination & Gene Ingeneering (Part III); comprehensive topics (Part IV). Totally 180 teaching hours, including 113 for theory and 45 for experiment and 22 individual sdudy. In this syllabus, the contents of 16 chaptesr have been pointed out what kind of demands should be met in different classes. That is----- emphasis means to memorize the knowledge basing on the understanding of the principle and to solve problems and practice applying the principle; difficulty means: not the emphasis but understand. The Teaching of Theory Chapter 1 Proteins: 7hours

⒈ Master the composition of proteins: ⑴ Elementary composition ⑵ The structural units(monomer units) of proteins — amino acid (aa,) ⒉ Master structure of proteins: ⑴ the Basic structure of proteins——polypeptide chain The peptide bond is extremely important, since it is the main structural bond found in all protins. ⑵ The levels of protein structure: i. the primary structure--The amino acid sequence of the polypeptide chain(and the presence of disulfide bonds) of a protein is called the primary structure. ii. the secondary structure — conformations of polypeptide chains. ⒊ Know well tertiary structure —three-dimensional shape of proteins. The specific three-dimensional structure of the protein in solution is called its tertiary structure. This is built up from primary and secondary structures by means of a number of bonding forces⑴hydrogen bond;⑵electrostatic bonds(salt links);⑶hydrophobic interactions between hydrophobic R groups;⑷disulfide bonds between cysteine residues. ⒋ Master the amphoteric properties and isoelectric point (pI). ⒌ Master the macromoleculer and colloidal behavior of protein solutions. ⒍ Know well denaturation of proteins. ⒎ Know well precipitation of proteins. ⑴ Salting out :The addition of high concentrations of neutral salts, such as (NH 4)2SO4, Na2SO4, or NaCl, to an

aqueous solution of protein causes it to preciptate. This phenomenon is referred to as salting out. ⑵ Organic solvents ⑶Heavy metals ⑷Certain acids ⒏ Understand the classification of proteins ⑴ Simple protein ⑵ Conjugated protein Emphasis: composition of proteins, structure of proteins, functions of protein. Difficulty: structure of proteins. Contents: composition of proteins, structure of proteins, propeties of proteins, fungction of proteins.

Chapter 2 Nucleic Acids: 8 hours ⒈ Master the composition of nucleic acids 1. elementary composition. 2. hydrolysis products of nucleic acids. The monomer units of nucleic acids are nucleotides. The basic componets of a nucleotide are nitrogenous base, pentose, phosphoric acid. 3. pentose sugars: ribose (only RNA) and 2-deoxyribose (only DNA). 4. nitrogenous bases The DAN molecule contains A,G,C,and T, whereas RNA molecules contain A,G.C and U. Notice that T occurs only in DNA and U occurs only in RNA. 5. Nucleosides A nucleotide is a phosphate ester of a nucleoside in which a molecule of phosphoric acid is esterified with one of the free hydroxyl group of the pentose sugar. ⒉ Master the structure of nucleic acids 1. The basic structure of nucleic acids —polynucleotide chain. The monoucleotides in DNA and RNA are linked by 3’-5’-phosphodiester bonds. The sequence of the nucleotides in polynucleotide strand is celled primary structure of nucleic acid. 2. The structure of DNA : the base composition of DNA; Chargaff,s rules; Waston-Crick model. 3. The structure of RNA: structure and function of mRNA; structure and function of tRNA and structure and function of rRNA; base pair rules. The secondary structure of tRNA—cloverleaf model. ⒊ Know well the properties of nucleic acids. 1. denaturation and renaturation of DNA. 2. renaturation and hybridization. 3. ultraviolet absorption. Emphasis: composition, structure and function of nucleic acid. Difficulty: structure and properties of nucleic acid. Contents: composition of nucleic acids, structure of nucleic acids, properties of nucleic acids, function of nucleic acids. Chapter 3 Enzymes 6 hours ⒈ Master conception of holoenzyme,coenzyme,active cente zymogen ,isoenzyme. ⒉ Master the character of enzyme catalyzed chemical reaction. ⒊ Master the structure and function of enzyme. ⒋ Know well kinetics of enzyme-catalyzed reactions

⒌ Understand classification and naming of enzyme. ⒍ Understand clinical applications of enzymes Emphasis: the structure and function of enzyme;the character of enzyme catalyzed chemical reaction. Difficulty: the structure and function of enzyme. Contents: concept of enzyme, the characters of enzyme catalyzed reaction, structure and function of enzyme, factors affecting enzyme action , allosteric enzyme and mechanism of allosteric enzyme in metabolism regulation, naming and classification of enzyme, enzyme and disease, application of enzyme in medicine . Chapter 4 Vitamins 4 1. Master the structure,coenzymes form and fungction of vitamins of B complex (water-soluble vitamins): VitaminB1, B2, pentothenic acid(B5), PP, B6, biotin, folic acid(B11), and B12. 2. Know well the function of Vitamin A , D , E ,and K ; Know well the function of Vitamin C. 3. Understand the vitamin deficiency disease. Emphasis: coenzymes form and function of vitamins of B complex. Difficulty: the structure of vitamins. Contents: Vitamin is defined as an essential, noncaloric, organic nutrient needed in tiny amounts in the diet. The role of many vitamins is to help make possible the processes by which other nutrients are digested, absorbed, and metabolized or built into body structures. Although small in size and quantity, the vitamins accomplish mighty tasks, some of which are still being discovered. Chapter 5 Carbohydrates Metabolisms 10

1. Master the glucose oxidized without oxygen. 2. Master the aerobic oxidation of glucose. 3. Master the pentose phosphate pathway. 4. Master the gluconeogenesis. 5. Know well the glycogenesis and glycogenolysis. 6. Understand blood sugar (glucose) and its regulation. Emphasis: Glucose oxidized without oxygen;aerobic oxidation of carbohydrate; pentosephosphate pathway;gluconeogenesis Difficulty:glucose oxidized without oxygen; aerobic oxidation of carbohydrate; gluconeogenesis and Its regulation Contents:carbohydrates, its chemical nature is polyhydroxyaldehyde or polyhydroxy-ketone and its derivant or polymerizer.Being oxidated to provide energy.Carbohydrates are the major source of energy for living organisms. This is its main function. Provide the material for other compounds when they are synthesized in vivo.For example, it provides material for synthesis of certain amino acids, lipids, cholesterol and nucleoside etc. As the component of cell in tissue. Carbohydrate is the component of glycoproteins, proteoglycans and glycolipids etc Chapter 6 Biological Oxidation 7 hours 1. Master conception of respiratory chain, oxidative phosphorylation, P/O ratio, ATP synthase. 2. Master complexes of the electron transport chain 3. Know well the utilization and storage of ATP. 4. Understand the definition and characteristics of biological oxidation. 5. Understand other biological oxidations Emphasis: conception of respiratory chain,oxidative phosphorylation,P/O ratio,ATP synthase. complexes of the electron transport chain Difficulty: complexes of the electron transport chain

Contents: conception of biological oxidation, electron transport chain and oxidative phosphorylation, energy from cytosolic NADH, other Biological oxidations Chapter 7 Metabolism of Lipids 10 hours 1. Master conceptions of HSL, ketone bodies, LPL, LCAT,ACAT 2. Master lipid transportation, fatty acid oxidation and ketone bodies metabolism. 3. Know well phospholipids and cholesterol metabolism. 4. Know well degradation of triacylglycerols, metabolism of cholestrols 5. Understand the function , digestion and absorption of lipid. 6. Understand the synthesis of fatty acids and triacylglycerol. Emphasis: lipid transportation, fatty acid oxidation,ketone bodies metabolism. Difficulty: lipid transportation, fatty acid oxidation and ketone bodies metabolism. Contents: digestion and absorption, digestion of dietary Lipids , metabolism of triacylglycerols , important derivatives of unsaturated fatty acids arachidonic acid , metabolism of phospholipids , metabolism of cholestrols,plasma lipids, metabolism of plasma lipoproteins. Chapter 8 Catabolism of Proteins 10 hours 1. Master conceptions of essential amino acid,one carbon unit. 2. Know well deamination of amino acids, decarboxylation of amino acids, metabolism of ammonia 3. Undestand degradation of protein in cells Emphasis : (1) The common metabolism of amino acids , including deamination of amino acids, metabolism of ammonia and metabolism of the carbon skeleton of amino acids. (2) The relationship among amino acid, glucose and fat metabolism. (3) The source、transportation and outlets of blood ammonemia. Difficulty: (1)Special amino acid metabolism and their important physical active substance. (2) The relationship among amino acid, glucose and fat metabolism Contents: 1.Nutritional Function of Proteins:Nutritional Requirement of Protein;Nutritional Quality of Proteins 2. Digestion, Absorption and Putrefaction (1) Digestion of fietary protein (2) Absorption and transportation of amino acids 3. Degradation of Protein in Cells (1)Lysosomal pathway (2)Cytosol pathway 4. Amino Acid Catabolism: General (1)Deamination of amino acids (2) Metabolism of ammonia (3) Metabolism of the carbon skeleton of amino acids 5 .Amino Acids Catabolism: Individual (1) Decarboxylation of amino acids (2) Metabolism of one carbon units (3)Metabolism of methionine, cysteine and cystine (4) Metabolism of aromatic amino acids (5) Degradation of branched-chain amino acids Chapter 9 Nucleotides Metabolism 6 hours 1. Master the sources of the nitrogen and carbonatoms of the purine ring

2. Master conversion of IMP to AMP and GMP 3. Master the sources of the nitrogen and carbonatoms of the pyrimidine ring 4. Master de novo synthesis of pyrimidine nucleotides 5. Master deoxyridonucleotide biosynthesis 6. Know well regulation of de novo Synthesis of purine nuceotides 7. Know well the salvage synthesis of purine nucleosides 8. Know well regulation of de novo synthesis of pyrimidine nucleotide 9. Undersand the biosynthetic pathway for inosine monophosphate(IMP) 10. Undersand the degrandation metabolism of purine nucleotides 11. Undersand the salvage synthesis of pyrimidine nucleotides Emphasis: the sources of the nitrogen and carbonatoms of the purine ring and the pyrimidine ring Difficulty: regulation of de novo synthesis of purine nuceotides Contents: 1.Functions of Nucleotides 2. Nucleotide Synthesis and Degradation (1) Metabolism of purine nucleotides (2) Metabolism of pyrimidine nucleotides (3) Deoxyribonucleotide biosynthesis (4) Biosynthesis of nucleoside diphosphate and nucleoside triphosphate 3. Dysmetabolism of nucleotides and antimetabolites (1) Dysmetabolism of nucleotides (2) Antimetabolites Chapter 10 Biosynthesis of DNA 6 hours 1.Master the conceptions of DNA replication, reverse transcription 2.Memorize the eukaryotic enzymes of DNA replication, recombination and repair 3.Undestand the process of replication Emphasis: (1)The basic principle of DNA replication (2)Enzymology of DNA replication (3)Mechanism of DNA repair Difficulty: (1)Enzymology of DNA replication (2)Formation of the replication fork (3)The process of DNA biological synthesis (replication) (4)Telomerase and telomere Contents: 1 .Overlook of DNA Replication: (1) DNA semiconservative replication (2) The general character of DNA replication 2. DNA replication in eukaryotic cells (1) Eukaryotic enzymes of DNA replication (2)Process of DNA replication in the eukaryotes (3)Telomere DNA replication (4)Mitochondrial DNA replication (5)Reverse transcription 3 .Prokaryotic DNA Replication (1)Prokaryotic enzymes and proteins involved in the DNA replication (2)Process of proeukaryotic replication

4 Recombination and Repair (1) Recombination of DNA (2) Gene mutation (3) DNA damage (4) Repair of DNA damage Chapter 11 Synthesis of RNA 7 hours 1.Master conceptions of asymmetric transcription ,structural gene ,operon, cos-acting element , ribozyme. 2.Memorize RNA polymerase of eukaryotic and prokaryotes; posttranscriptional modification in eukaryotic transcription 3.Undestand RNA synthesis Emphasis: (1)The template, enzymes and processing of RNA biological synthesis. (2)Post-transcriptional modification in eukaryotes. (3)Enzymes involved in transcription (4)RNA pol in eukaryotes Difficulty: (1)Enzymes involved in transcription (2)Process of transcription (3)Termination of initiation (4)Post- transcriptional processing in eukaryotes Contents: 1 .RNA Synthesis in Prokaryotes (1) RNA polymerase (2) Initiation of RNA synthesis (3) Elongation of RNA synthesis (4) Termination of RNA synthesis (5) Posttranscriptional modification 2. RNA Synthesis in eukaryotes (1)Three types of RNA polymerase in eukaryotic transcription (2) Initiation of RNA synthesis in eukaryotic transcription (3) Elongation and termination of transcription in eukaryotic transcription (4)Posttranscriptional modification in eukaryotic transcription (5) RNA degradation 3. Reverse Transcription and RNA Replication (1) Reverse transcription (2) RNA replication

(3) RNA based evolution
Chapter 12 Biosynthesis of Protein 6 hours 1.Master the conceptions of cistron,genetic coden,open eading frame,wobble signal epetide 2.Memorize the components of protein biosynthesis, posttranslational processing, 3.Undestand the steps of protein biosynthesis, clinical correlation of protein biosynthesis Emphasis: (1)Materials involved in the translation

(2)The process of synthesis Difficulty: (1)Function of nucleic acid in the process of protein biosynthesis (2)Fundamental procedure of protein biosynthesis (3)Processing after translation Contents: 1. Components of protein biosynthesis (1) Messenger RNA (2) Amino acids and tRNAs (3) rRNAs and ribosomes (4) Aminoacyl-tRNA synthetases 2. Steps of Protein Biosynthesis (1) Initiation of protein biosynthesis (2) Elongation of polypeptide chain (3) Termination of protein biosynthesis (4) Energy cost for protein biosynthesis 3. Posttranslational Processing (1) Posttranslational modification (2) Folding of newly synthesized polypeptides (3) Protein targeting 4. Clinical correlation of protein biosynthesis (1) Molecular diseases (2)Effect of antibiotics on protein biosynthesis (4) Effect of some biologically active molecules on protein biosynthesis

Chapter 13

Regulation of Gene Expression 7 hours

1.Master conception of gene control 2.Memorize basic elements in the tTranscription activation;regulation of gene transcription in prokaryotes amd eukaryotes 3.Undestand basic principles of gene control Emphasis: Regulation of gene transcription in prokaryotes; gene expression can be regulated at many of the steps. Difficulty: Regulation of gene transcription in prokaryotes Contents: 1. Basic Principles of Gene Control (1) The concept of gene expression (2)Temporal specificity and spatial specificity of gene expression (3)The constitutive expression and the inducible expression (4) Gene expression can be regulated at many of the steps. (5) Basic elements in the transcription activation: 2 .Regulation of Gene Transcription in prokaryotes (1) Regulation of transcription initiation in prokaryotes (2) Regulation of the lactose system (The Jacob-Monod Model) (3) Regulation of tryptophan production 3. Regulation of Transcription in Eukaryotes (1) Characteristics of gene regulation in eukaryotes

(2) Transcription activation in eukaryotes

Chapter 14 Gene Recombinant & Gene Ingeneering 8 hours
1.Master the conceptions of Genetic Engineering 2.Know well the Common Tools Used in Genetic Engineering Emphasis: Processes of genetic engineering; related concept Difficulty: Processes of genetic engineering Contents:Related concept:DNA clone;Tool enzyme;Target gene;Gene vector; Relationship of recombinant DNA technique and medicine;common tools used in genetic engineering;Processes of genetic engineering

Chapter 15 Blood Biochemistry

5 hours

1.Master the precursors and the key enzyme of the heme’s synthesis 2.Known well classification and characters of plasma proteins 3. Known well function of the plasma proteins 4. Known well biochemical features of red blood cells 5.Undestand biochemical features of white blood cells Emphasis:Synthesis and Regulation of heme Difficulty: Synthesis of heme Contents: Composition and function of blood, classification and characters of plasma proteins,the function of the plasma proteins, biochemical features of red blood cells.biochemical features of white blood cells. Chapter 16 Liver Biochemistry 6 hours 1.Master the conception of biotransformation ,primary bile acid,seconday bile acid. 2. Master the conception of the enterohepatic circulation of bile acid. 3. Known well the important role of liver in material metabolism. 4.Known well the hepatic biotransformation and bile pigment Metabolism and Jaundice 5.Undestand the metabolism of the bile and the bile acid: Emphasis: Hepatic biotransformation, the enterohepatic circulation of bile acid. Difficulty: The metabolism of the bile and the bile acid. Contents:The important role of liver in material metabolism, hepatic biotransformation, the metabolism of the bBile and the bile acid, bile pigment metabolism and jaundice .

The Teaching of Practice Experiment 1 Protein determination by the biuret reaction

5 hours

1. Emphasis (1).Master the rules of biochemical laboratory and the basic contents of the experimental report (2).Master the principle of spectrophotometry (3).Master the biuret method to determine protein 2. Contents of practice (1). Plot the standard curve (2). Unkown sample determination 3. Homework

Experiment 2 The effect of substrate concentration on the activity of alkalin phosphatase and

thedetermin –action of Km of alkaline phosphatase

(Its abbreviation is AKP) 5 hours 1.Master the method of determination of Km of alkaline phosphatase 2. Master the significance of Km 3. Master the effect of substrate concentration on the activity of AKP 4. Known well how to design an experiment of enzyme Homework: Make Linewearver-Burk plot with 1/[S] as abscissa and 1/V as the ordinate (of 1/v versus 1/[S]), Read 1/Km from the beeline,then calculate Km. Experiment 3 The Effect of Adrenalin and Insulin on Concentration of Blood Sugar 1. Emphasis: (1) Master the method of determination concentration of blood sugar (2) Know well the effect of adrenalin and insulin on concentration of blood sugar 2. Contents of practice (1)Separately weigh 2 rabbits (2)Separately draw the blood from 2 rabbits (3)Inject insulin and adrenaline (4)Again separately draw the blood (5)Prepaire protein—free filtrates (6)Determination of Glucose by the method of Folin and Wu. (7)Result 5 hours

Experiment 4 The Separation of Serum Protein by Cellulose Acetate Membrane Electrophoresis 5 hours 1. Emphasis: (1) Master the method of Cellulose Acetate membrane electrophoresis. (2) Know well the classification of serum protein by electrophoresis. (3) Understand the principle of electrophoresis. 2. Contents: (1) Preparation:soak the membranes (2) Sample application (3) Electrophoresis (4) Staining and rinsing (5) Result: draw the results on the report book Experiment 5 Isolation and Determination of Nucleic Acid 5 hours 1.Master the principle and procedure of isolation and determination of RNA 2. Master the usage of spectrophotometer ,pipette and centifuge. 3. Kown well preparation of homogenate. 4. Undestand the distributing of DNA and RNA. 5.Emphasis:Nucleotid metabolism (Functions of nucleotid\ Metabolism of purine\metabolism of pyrimidine) 6. Emphasis :process of nucleotid pickup 7. Contents of practice (1) Samples :rabbil liver (2) Preparation homogenateof liver (3) Centrifual extraction :wipe off piotein ,deposited nucleotid (6) To write the experiment report

Experiment 6 Isolation and Purification of serum γ-globulins 5 hours 1.Emphasis:master the three methods to isolation and purification of protein: salting out, gel filtration chromatography and ion exchange chromatography 2.Contents of practic (1). Rough isolation by salting out (2). Desalting by gel filtration (3). Purification by ion exchange chromatography 3. Homework Write experiment report Reference Books : 1. Zhou Airu. 2004. Biochemistry (Chinese). 6th Edition. Beijing: Renmin Weisheng publisher 2. Berg J M,Tymoczko J L,Stryer L. 2002. Biochemistry. 5th Edition. New York:W.H. Freeman Publishers 3. Chytil F, Mccmick D B .1986. Vitamins and coenzymes. New York: New York Halsted Press 4. Devlin T M.. 2002. Textbook of Biochemisrty with Clinical Correlations, New York: Wiley-Liss 5. Robert K. Murray, Daryl K. Granner, Peter A. Mayes , et al. 2000. Harper’s Biochemistry. 25th Edition. Stamford:McGraw-Hill


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