PURIFICATION OF GLYOXALASE-I FROM HUMAN ERYTHROCYTES BY THE USE OF AFFINITY CHROMATOGRAPHY AND SEPARATION OF THE 3 ISOENZYMES

被引：48

作者：

ARONSSON, AC

TIBBELIN, G

MANNERVIK, B

机构：

[1] Department of Biochemistry, Arrhenius Laboratory, University of Stockholm

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 92卷 / 02期

关键词：

D O I：

10.1016/0003-2697(79)90676-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Glyoxalase I has been purified to homogeneity from human erythrocytes. An essential part in the purification procedure involved affinity chromatography on S-hexylglutathione bound to epoxy-activated Sepharose 6B. Three isoenzymes were found, which could be separated by ion-exchange chromatography. Some of the properties of the enzyme are reported. © 1979.

引用

页码：390 / 393

页数：4

共 10 条

[1]

Andrews P, 1970, Methods Biochem Anal, V18, P1, DOI 10.1002/9780470110362.ch1

[2] CHARACTERIZATION OF GLYOXALASE-I PURIFIED FROM PIG ERYTHROCYTES BY AFFINITY CHROMATOGRAPHY [J].