INTERFACIAL ENZYMOLOGY OF PHOSPHOLIPASE-A2

被引：29

作者：

GELB, MH

JAIN, MK

BERG, O

机构：

[1] UNIV WASHINGTON,DEPT BIOCHEM,SEATTLE,WA 98195

[2] UNIV DELAWARE,DEPT CHEM & BIOCHEM,NEWARK,DE 19716

[3] UNIV UPPSALA,CTR BIOMED,DEPT MOLEC BIOL,S-75123 UPPSALA,SWEDEN

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1992年 / 2卷 / 11期

关键词：

D O I：

10.1016/S0960-894X(00)80508-9

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Methods have been recently developed to analyze the phospholipase A2-catalyzed hydrolysis of phospholipid aggregates in terms of standard kinetic theory. It is now possible to extract the Michaelis-Menten parameters, to determine the interfacial equilibrium constants for the binding of inhibitors and substrates to the active site of the enzyme bound to the interface, and to determine relative substrate preferences in the interface.

引用

收藏

页码：1335 / 1342

页数：8

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