AMIDASIC ACTIVITY OF NEPSILON-ACETYLTRYPSIN FREE OR BOUND ON ALPHA2 MACROGLOBULIN

被引：13

作者：

JACQUOTARMAND, Y

KREBS, G

机构：

[1] Laboratoire de Biologie Physico-Chimique, Faculté des Sciences

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 36卷 / 05期

关键词：

D O I：

10.1016/0006-291X(69)90682-2

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：

Nε-acetyltrypsin (Tac) exhibits a higher activity than native trypsin towards an amide substrate, Nα-benzoyl dl-arginine p-nitroanilide (BAPA). Affinity constants for the substrate are not modified but the rate constant is increased five times. A complex is formed between Tac and the α2 macroglobulin (αM) in the same conditions as we have seen for native trypsin: 1 mole of αM binds to 2 moles of enzyme. The increase of Tac activity towards BAPA disappears once a stable complex is formed. Possible explanations for these observations are discussed. © 1969.

引用

页码：815 / +

页数：1

共 11 条

[1] MISE EN EVIDENCE DUN EFFET ALLOSTERIQUE LORS DE LHYDROLYSE DU P-TOLUENE SULFONYL-L-ARGINYL-METHYL ESTER PAR LA TRYPSINE [J].