ON SOME AUTOLYZED DERIVATIVES OF BOVINE TRYPSIN

被引：63

作者：

MAROUX, S

DESNUELLE, P

机构：

[1] Centre de Biochimie et de Biologie Moléculaire, C.N.R.S., Marseille

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 181卷 / 01期

关键词：

D O I：

10.1016/0005-2795(69)90227-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Chromatography or incubation of dilute solutions of bovine trypsin at 4° and pH 5.5 in the presence of Ca2+ appears to induce almost exclusively the autolytic cleavage of bond Arg105-Val106. Bonds Lys49-Ser50 and Lys131-Ser132 are also found substantially autolyzed in commercial trypsin preparations. Evidence is presented suggesting that trypsin still retain activity after cleavage of bonds Arg105-Val106 and Lys131-Ser132. In contrast, the cleavage of bond Lys49-Ser50, close to residue His46, probably inactivates the enzyme. © 1969.

引用

页码：59 / +

页数：1

共 23 条

[1]

CRESTFIELD AM, 1963, J BIOL CHEM, V238, P622

[2]

DAVIE EW, 1955, J BIOL CHEM, V212, P515

[3]

DELAAGE M., 1965, BIOCHIM BIOPHYS ACTA, V105, P608

[4] SUR LA SEQUENCE N-TERMINALE DU TRYPSINOGENE ET SON ABLATION PENDANT LACTIVATION DE CE ZYMOGENE [J].