PURIFICATION OF S-2-HYDROXYACYLGLUTATHIONE HYDROLASE (GLYOXALASE-II) FROM RAT ERYTHROCYTES

被引：39

作者：

BALL, JC

VANDERJAGT, DL

机构：

[1] UNIV NEW MEXICO,DEPT BIOCHEM,ALBUQUERQUE,NM 87131

[2] UNIV NEW MEXICO,DEPT CHEM,ALBUQUERQUE,NM 87131

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 98卷 / 02期

关键词：

D O I：

10.1016/0003-2697(79)90169-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Glyoxalase II, a specific glutathione thiolesterase, has been purified 9100-fold from rat erythrocytes using a purification scheme which employs Affi-Gel blue as a hydrophobic affinity column and also employs a glutathione-affinity column prepared by coupling S-(p-chlorophenacyl)glutathione to Affi-Gel 202. This procedure offers a convenient method for the preparation of highly purified glyoxalase II. Also described is a convenient method for the preparation of S-lactoyl-glutathione, a substrate for glyoxalase II. © 1979.

引用

页码：472 / 477

页数：6

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