PURIFICATION OF GLUTATHIONE S-TRANSFERASES FROM RAT LUNG BY AFFINITY CHROMATOGRAPHY - EVIDENCE FOR AN ENZYME FORM ABSENT IN RAT-LIVER

被引：86

作者：

GUTHENBERG, C

MANNERVIK, B

机构：

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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 86卷 / 04期

关键词：

D O I：

10.1016/0006-291X(79)90258-4

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：

Glutathione S-transferases from rat lung cytosol were purified about 200-fold in one step by chromatography on S-hexylglutathione bound to epoxy-activated Sepharose 6B. Further purification on hydroxyapatite resolved the lung transferases into five peaks of activity as measured with 1-chloro-2,4-dinitrobenzene as substrate. Three of the peaks were identified with transferases A, B, and C of rat liver on the basis of chromatographic properties, immunochemical reactivity, and substrate specificity. The other two activity peaks were not detectable in liver: one originated from the lung tissue and one appeared to result from blood in the lung. © 1979.

引用

页码：1304 / 1310

页数：7

共 15 条

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