生物化學(xué)

內(nèi)容概要

　　《生物化學(xué)》是雙語教材，總結(jié)多年教學(xué)中沉淀的經(jīng)驗，按照醫(yī)學(xué)各專業(yè)的特點，將生物化學(xué)劃分為生物大分子的結(jié)構(gòu)與功能、物質(zhì)代謝、基因表達和專題篇4個部分，努力構(gòu)建系統(tǒng)化課程，從學(xué)生興趣、認知規(guī)律和探究方便出發(fā)合理設(shè)計教材的結(jié)構(gòu)，注意聯(lián)系實際，適度擴大學(xué)生的知識面和應(yīng)用能力，突出教材中知識結(jié)構(gòu)的科學(xué)化。并以鮮活靈動的色彩、圖文并茂的版面、熟悉的例子吸引剛?cè)腴T的醫(yī)學(xué)生，讓學(xué)生感受課程學(xué)習(xí)的趣味性和挑戰(zhàn)性，將是一系統(tǒng)性強、可讀性強、深受學(xué)生喜愛的教材。

書籍目錄

PART Ⅰ : STRUCTURE AND FUNCTION OF BIOMACROMOLECULEChapter 1 Structure and Function of ProteinSECTION 1 THE COMPOSITION OF PROTEIN1.1 Amino acid1.2 Peptide1.3 Some small polypeptides have biological activitySECTION 2 MOLECULAR STRUCTURE OF PROTEINS2.1 Primary structure2.2 Secondary structure2.3 Tertiary structure2.4 Major noncovalent bond2.5 Quaternary structureSECTION 3 RELATION BETWEEN STRUCTURE AND FUNCTION OF PROTEINS3.1 Primary structure and potential function of protein3.2 Spatial structure shows the function of proteinSECTION 4 CHEMICAL AND PHYSICAL PROPERTIES OF PROTEINS4.1 Ultraviolet absorption spectrum of protein4.2 Isoelectric point (pI)4.3 Denaturation of proteinSECTION 5 ISOLATION, PURIFICATION AND SEQUENCING OF PROTEINS5.1 Dialysis and ultrafiltration5.2 Precipitation with acetone, salting precipitation and immunoprecipitation5.3 Chromatographic separations5.4 Electrophoresis5.5 UltracentrifugationSUMMARYChapter 2 Chemistry of Nucleic AcidsSECTION 1 MOLECULAR COMPOSITION OF NUCLEIC ACIDS1.1 Basic components1.2 Nucleosides1.3 MononucleotidesSECTION 2 MOLECULAR STRUCTURES OF DNA2.1 Primary structure of nucleic acid2.2 Chargaff's rules2.3 Secondary structure of DNASECTION 3 PHYSICO-CHEMICAL PROPERTIES OF NUCLEIC ACIDS3.1 Viscosity3.2 Ultraviolet absorption3.3 Denaturation and renaturation of DNA3.4 Hydrolysis of acid or alkaliSECTION 4 STRUCTURES OF RNA4.1 Messenger RNA4.2 Transfer RNA4.3 Ribosomal RNASUMMARYChapter 3 EnzymesSECTION 1 THE MOLECULAR COMPOSITION AND FUNCTION OF ENZYMES1.1 The molecular composition of enzymes1.2 The active center of enzymes1.3 Many enzymes require cofactorsSECTION 2 PROPERTIES AND MECHANISM OF ENZYME CATALYSIS2.1 Remarkable properties of enzymes2.2 Mechanism of enzyme catalysisSECTION 3 THE KINETICS OF ENZYME CATALYSIS3.1 Catalysis occurs at the active site3.2 Multiple factors affect the rates of enzyme-catalyzed reactions3.3 Initial rate is proportionate to enzyme concentration3.4 Substrate concentration affects reaction rate3.5 The Michaelis-Menten equations model the effects of substrate concentration3.6 Kinetic analysis distinguishes competitive from noncompetitive inhibitionSECTION 4 ZYMOGENS AND ISOZYMES4.1 Zymogens and zymogen activation4.2 Isozymes are physically distinct forms of the same catalytic activitySECTION 5 THE NAME AND CLASSIFICATION OF ENZYMES SECTION 6 THE QUANTITATIVE ANALYSIS OF CERTAIN PLASMA ENZYMES IS OF DIAGNOSTIC SIGNIFICANCE 6.1 Low levels of nonfunctional plasma enzymes result from normal destruction of cells 6.2 Nonfimcfional plasma enzymes aid diagnosis and prognosis SUMMARY PART Ⅱ:METABOLISM Chapter 4 Metabolism of Carbohydrate SECTION 1 DIGESTION OF DIETARY CARBOHYDRATES SECTION 2 GLYCOLYSIS 2.1 Concept ofglycolysis 2.2 Glycolytic pathway 2.3 Regulation ofglycolysis 2.4 Lactate metabolism SECTION 3 THE PYRUVATE DEHYDROGENASE COMPLEX AND THE CITRIC ACID CYCLE 3.1 The pyruvate dehydrogenase complex 3.2 Regulation of the PDH complex 3.3 Reactionsofthe tricarboxylic acid cycle SECTION 4 PENTOSE PHOSPHATE PATHWAY 4.1 Reactions of the pentose phosphate pathway 4.2 The functions of this pathway 4.3 Erythrocytes and the pentose phosphate pathway 4.4 Pentose phosphate pathway with disease SECTION 5 GLYCOGEN METABOLISM 5.1 Glycogen synthesis 5.2 Glyeogenolysis 5.3 The functions ofglycogenesis and glycogenolysis SECTION 6 GLUCONEOGENESIS 6.1 Gluconeogenesis 6.2 Regulation of gluconeogenesis SECTION 7 REGULATION OF BLOOD SUGAR LEVELS SUMMARY Chapter 5 Biological Oxidation SECTION 1 THE WAY OF OXIDATION 1.1 Additionofoxygen 1.2 Removal of electrons 1.3 Dehydrogenation SECTION 2 RESPIRATORY CHAIN 2.1 The composition of respiratory chains 2.2 Two capital kinds of respiratory chains 2.3 Oxidative phosphorylation 2.4 Factors of influence on oxidative phosphorylation 2.5 Shuttle systems are required for mitochondrial oxidation ofcytosolic NADHSUMMARY Chapter 6 Lipid Metabolism SECTION 1 DIGESTION AND ABSORPTION OF LIPIDS SECTION 2 BLOOD LIPIDS AND LIPOPROTEINS 2.1 The composition and content of blood lipoprotein 2.2 The classification of lipoproteins SECTION 3 INTERMEDIATE METABOLISM OF TRIACYLGLYCEROLS 3.1 Hydrolysis oftriacylglycerols in adipose tissue 3.2 Oxidation of fatty acids 3.3 Fatty acid synthesis 3.4 Biosynthesis oftriacylglycerol SECTION 4 METABOLISM OF PHOSPHOLIPIDS SECTION 5 CHOLESTEROL METABOLISM 5.1 Biosynthesis of cholesterol 5.2 Transformation and excretion of cholesterol SUMMARY Chapter 7 Amino Acid Metabolism SECTION 1 NUTRITION OF PROTEINS 1.1 Nutrition of the proteins 1.2 Nitrogen balance and protein requirements 1.3 The biosynthetic pathways of amino acids SECTION 2 DIGESTIONANDABSORPTION OF PROTEINS 2.1 Protein turnover occurs in all forms of life 2.2 Proteases and peptidases degrade proteins to amino acids SECTION3 AMINO ACID CATABOLISM 3.1 Overall view 3.2 Deamination ofarnino acids 3.3 Metabolism of the carbon skeletons of amino acids SECTION 4 METABOLISM OF AMMONIA 4.1 Sources and disposals of blood ammonia 4.2 Transport of ammonia 4.3 Inter-organ exchange maintains circulating levels of amino acids ……PART Ⅲ:GENE EXPRESSINGPART Ⅳ:SPECIAL TOPICS

章節(jié)摘錄

插圖：which is a destabilizing influence. As a result, a helices are often capped at the N-terminal end by a negatively charged amino acid （like glutamic acid） in order to stabilize the helix dipole. Less common （and less effective） is C-terminal capping with a positively charged amino acid like lysine. This is because of a structural coincidence: The diameter of the α-helix is 120 nm, the same as the width of the major groove in B-form DNA.2.2.2 β-pleated sheetAfter the discovery of helix, Panling and Corey discovered that polypeptide chains could fold in another way, which they named beta-pleated sheet （beta is second, alpha was first）. The β sheet （also called 13-pleated sheet） is a commonly occurring form of regular secondary structure in proteins, first proposed by Linus Panling and Robert Corey in 195L The β-pleated sheet is composed of two or more straight chains that are hydrogen bonded side by side （Fig.l-9）. If the amino termini are on the same end of each chain, the sheet is termed parallel, and if the chains run in the opposite direction （amino termini on opposite ends）, the sheet is termed antiparallel.In this case more H-bonding is achieved by stretching out the polypeptide chain, and laying it side by side to form H-bonds between lengths of polypeptide chain. Thus providing both inter and intra-H bonds. The structure is called a beta-pleated sheet because of the serrated zig appearance when viewed from the side. Substantially different from the α-helix in that it is a sheet rather than a rod and polypeptide chain is fully stretched rather than tightly coiled as in helix. The H-bonds are formed from amino and carboxyl groups as for a-helix, but bonding also occurs between different stands of a polypeptide.The stands can run in opposite directions to give antiparallel beta-pleated sheets or they can run in the same direction to give parallel beta-pleated sheets. Beta sheets occur in variable　amounts in the polypeptide chains of globular proteins.

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《生物化學(xué)》是高等醫(yī)藥院校雙語教材之一。

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