INACTIVATION OF HUMAN PLACENTA GLUTATHIONE-S-TRANSFERASE BY SH SS EXCHANGE-REACTION WITH BIOLOGICAL DISULFIDES

被引：51

作者：

NISHIHARA, T

MAEDA, H

OKAMOTO, K

OSHIDA, T

MIZOGUCHI, T

TERADA, T

机构：

[1] Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University, Suita, Osaka, 565

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 174卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91456-M

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 oxidized glutathione inhibited the activity of glutathione S-transferase purified from human placenta just through competitive inhibition. On the other hand, cystine and cystamine inactivated the activity by pseudo first-order in low concentrations, accompanying the stoichiometric incorporation of the radioactivity of [14C]-cystine to the enzyme protein until a half mole per one subunit. This and the protective effect of glutathione analogues suggested that the SH SS exchange reaction occurred between the disulfide and the SH group near the glutathione binding site of the enzyme to form a mixed disulfide. © 1991.

引用

页码：580 / 585

页数：6

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