THE PRINCIPAL DIFFERENCE IN REGULATION OF THE CATALYTIC ACTIVITY OF WATER-SOLUBLE AND MEMBRANE FORMS OF ENZYMES IN REVERSED MICELLES - GAMMA-GLUTAMYL-TRANSFERASE AND AMINOPEPTIDASE

被引：11

作者：

KABANOV, AV

NAMETKIN, SN

LEVASHOV, AV

机构：

[1] Department of Chemical Enzymology, Moscow State University, Moscow

来源：

FEBS LETTERS | 1990年 / 267卷 / 02期

关键词：

Aminopeptidase; Micellar enzymology; Reversed micelle; γ-Glutamyltransferase;

D O I：

10.1016/0014-5793(90)80933-A

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：

The regularities of their functioning of enzyme, water-soluble and membrane forms, in the systems of the reversed micelles of surfactants in organic solvents are compared. Using as examples γ-glutamyltransferase (in AOT reversed micelles in octane) and aminopeptidase (in Brij 96 reversed micelles in cyclohexane), the principal difference in the catalytic activity regulation of water-soluble and membrane forms is demonstrated. The catalytic activity of the membrane form depends considerably on the surfactant concentration at the constant degree of hydration, whereas the activity of the water-soluble form is constant under these conditions. The catalytic activity dependence on the surfactant concentration is regarded as a test for enzyme membrane activity. © 1990.

引用

页码：236 / 238

页数：3

共 19 条

[1]

[Anonymous], 1989, STRUCTURE REACTIVITY

[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] AN AMINOPEPTIDASE FROM BOVINE BRAIN WHICH CATALYZES THE HYDROLYSIS OF ENKEPHALIN [J].