《蛋白质与酶学研究》求取 ⇩

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