图书介绍

蛋白质与酶学研究PDF|Epub|txt|kindle电子书版本网盘下载

蛋白质与酶学研究
  • 邹承鲁 著
  • 出版社：
  • ISBN：
  • 出版时间：未知
  • 标注页数：313页
  • 文件大小：21MB
  • 文件页数：321页
  • 主题词：

PDF下载


点此进入-本书在线PDF格式电子书下载【推荐-云解压-方便快捷】直接下载PDF格式图书。移动端-PC端通用
种子下载[BT下载速度快]温馨提示：（请使用BT下载软件FDM进行下载）软件下载地址页直链下载[便捷但速度慢]  [在线试读本书]   [在线获取解压码]
点击复制MD5值：8d9e2f6c0154eb1c6fb01e88b4e85725

下载说明

蛋白质与酶学研究PDF格式电子书版下载

下载的文件为RAR压缩包。需要使用解压软件进行解压得到PDF格式图书。

点击复制85GB完整离线版磁力链接到迅雷FDM等BT下载工具进行下载  详情点击-查看共享计划
建议使用BT下载工具Free Download Manager进行下载,简称FDM(免费,没有广告,支持多平台）。本站资源全部打包为BT种子。所以需要使用专业的BT下载软件进行下载。如BitComet qBittorrent uTorrent等BT下载工具。迅雷目前由于本站不是热门资源。不推荐使用！后期资源热门了。安装了迅雷也可以迅雷进行下载！

（文件页数 要大于 标注页数，上中下等多册电子书除外）

注意：本站所有压缩包均有解压码： 点击下载压缩包解压工具

图书目录

Contents1

1．Respiratory Chain1

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 Enzymology38

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．Insulin52

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.35,1180

4．Kinetics of Irreversible Modification of Enzyme Activity192

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 Proteins285

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

热门推荐