- 作 者：邹承鲁
- 出 版 社：
- 出版年份：2222
- ISBN：
- 标注页数：313 页
- PDF页数：321 页
请阅读订购服务说明与试读!
订购服务说明
1、本站所有的书默认都是PDF格式，该格式图书只能阅读和打印，不能再次编辑。
2、除分上下册或者多册的情况下，一般PDF页数一定要大于标注页数才建议下单购买。【本资源321 ≥313页】
图书下载及付费说明
1、所有的电子图书为PDF格式，支持电脑、手机、平板等各类电子设备阅读；可以任意拷贝文件到不同的阅读设备里进行阅读。
2、电子图书在提交订单后一般半小时内处理完成,最晚48小时内处理完成。(非工作日购买会延迟)
3、所有的电子图书都是原书直接扫描方式制作而成。
Contents 1
1．Respiratory Chain 1
1.1．C．L．Tsou．Cytochrome c modified by digestion with pepsin.Nature,164,1134.(1949) 1
1.2．C．L．Tsou．Exogenous and endogenous cytochrome c.Bio-chem.J.50,493-499.(1952) 4
1.3．C．Y．Wu and C．L．Tsou．Studies on the codehydrogenase cytochrome c enzyme systems.Ⅰ.The simultaneous oxida-tion of succinate and reduced codehydrogenase.Sci.Sin.4,137-155.(1955) 11
1.4．T．Y．wang,C．L．Tsou and Y．L．Wang．Studies on suc-cinic dehydrogenase.Ⅰ.Isolation,purification and properties.Sci.Sin.5,73-90,(1956) 30
3．Chemical Modification of Proteins and Molecular Enzymology 38
3.1．C．L．Tsou．Relation between modification of functional groups of proteins and their biological activity.Ⅰ.A graphical method for the determination of the number and type of essential groups.sci.sin.11,1535-1558.(1962). 38
1.5．Y．Z．Jin,H．L．Tang,S．L．Li and C．L．Tsou．The triphasic reduction of cytochrome b in the succinate cytochrome c reductase.Biochim.Biophys.Acta,637,551-554.(1981) 48
2．Insulin 52
2.1．Y．C．Du,Y．S．Zhang，Z．X．Lu and C．L．Tsou．Resynthe-sis of insulin from its glycyl and phenylalanyl chains.Sci.Sin.10,84-104.(1961) 52
2.2．Collective work.The total synthesis of crystalline insulin.Kexue Tongbao,17,241-277.(1966) 73
2.3．C．C．Wang and C．L．Tsou．The interaction and reconsti-tution of carboxyl-terminal shortened B chains with the intact A chain of insulin.Biochemistry,25,5336-5340.(1986) 110
2.4．Z．X．Wang,M．Ju and C．L．Tsou．Number of ways of joining SH groups to form multi-peptide chain proteins.J.theor.Biol.124,293-301.(1987) 115
2.5．J．G．Tang,C．C．Wang and C．L．Tsou．Formation of native insulin from the scrambled molecule by protein disulfide-isomerase.Biochem,J.255,451-455.(1988). 124
2.6．C．C．Wang C．L．Tsou．The insulin A and B chains contain sufficient structural information to form the native molecule.TIBS,16,270-281.(1991) 129
2.7．J．Wei,L．Xie,Y．Z．Lin and C．L．Tsou．The pairing of the separated A and B chains of insulin and its deriva-tives,FTIR Studies.Biochim.Biophys.Acta.1120,69-74.(1992) 132
3.2．G．J．Xu and C．L．Tsou．Relation between modification of functional groups of proteins and their biological activity.Ⅱ.The number of essential disulfide linkages in trypsin.Acta Biochem.Biophys.Sin.163-168.(1963). 162
3.3．Y．S．Ho and C．L．Tsou．Formation of a new fluorophore on irradiation of carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase.Nature,277,245-246.(1979). 168
3.4．C．L．Tsou,G．Q．Xu,J．M．Zhou and K．Y．Zhao．A new fluorescent probe for the study of the allosteric proper-ties of D-glyceraldehyde-3-phosphate dehydrogenase.Biochem.Soc.Trans.11,425-429.(1983) 170
3.5．X．-C．Wang,H．-M．Zhou,Z．-X．Wang and C．L．Tsou．Is the Subunit the Minimal Function Unit of Creatine Kinase?Biochim.Biophys.Acta,1039,313-317(1990) 175
3.6．Z．R．Sun,K．Y．Zhao,Z．X．Wang,H．M．Zhou and C．L．Tsou．Quantitative relation between modification of functional groups of proteins and their biological acti-vity.A computer program for ascertaining the number of essential residues.Sci.sin.B.35,1 180
4．Kinetics of Irreversible Modification of Enzyme Activity 192
4.1．C．L．Tsou．Kinetics of irreversible modification of enzyme activity.1.The effect of substrate on the rate of binding between an enzyme and a modifier.Acta Bio-chim.Biophys.Sin.5,398-408.(1965) 192
4.2．C．L．Tsou．Kinetics of irreversible modification of enzyme activity.2.The substrate reaction during the course of modification.Acta Biochim.Biophys.sin.5,409-417.(1965) 203
4.3．W．X．Tian and C．L．Tsou．Determination of the rate constant of enzyme modification by measuring the sub-strate reaction in the presence of the modifier.Biochem-istry,21,1028-1032.(1982) 212
4.4．W．Liu,K．Y．Zhao and C．L．Tsou．Reactivation kinetics of diethylphosphoryl acetylcholine esterase.Eur.J.Biochem.151,525-529.(1985) 217
4.5．C．L．Tsou．Kinetics of substrate reaction during irre-versible modification of enzyme activity.Adv.Enzymol.61,381-436.(1988) 222
4.6．J．M．Zhou,C．Liu and C．L．Tsou．Kinetics of trypsin inhibition by its specific inhibitors.Biochemistry,28,1070-1076.(1989) 278
5．Folding and Unfolding of Proteins 285
5.1．Q．Z．Yao,M．Tian and C．L．Tsou．Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation.Biochemistry,23,2740-2744.(1984) 285
5.2．C．L．Tsou．Location of the active sites of some enzymes in limited and flexible molecular regions.Trends Bio-chem.sci.11,427-429.(1986) 290
5.3．G．F．Xie and C．L．Tsou．Conformational and activity changes during guanidine denaturation of D-glyceralde-hyde-3-phosphate dehydrogenase.Biochim.Biophys.Acta,911,19-24.(1987) 293
5.4．C．L．Tsou．Folding of the nascent peptide chain into a biologically active protein.Biochemistry,27,1809-1812.(1988) 299
5.5．Y．Z．Lin,S．J．Liang,J．M．Zhou,C．L．Tsou,P．Wu and Z．Zhou．Comparison of inactivation and conformational changes of D-Glyceraldehyde-3-phosphate dehydrogenase during thermal denaturation.Biochim.Biophys.Acta,1038.247-252.(1990) 303
5.6．Y．Z．Ma and C．L．Tsou．Comparison of the activity and conformation changes of lactate dehydrogenase H4 during denaturation by guanidinium chloride.Biochem.J.277,207-211.(1991) 309