HUMAN HEPATIC 3-ALPHA-HYDROXYSTEROID DEHYDROGENASE - POSSIBLE IDENTITY WITH HUMAN HEPATIC CHLORDECONE REDUCTASE

被引：10

作者：

BINSTOCK, JM

IYER, RB

HAMBY, CV

FRIED, VA

SCHWARTZ, IS

WEINSTEIN, BI

SOUTHREN, AL

机构：

[1] NEW YORK MED COLL,DEPT MED,VALHALLA,NY 10595

[2] NEW YORK COLL PODIATR MED,DEPT BIOCHEM,NEW YORK,NY 10035

[3] NEW YORK MED COLL,DEPT CELL BIOL & ANAT,VALHALLA,NY 10595

[4] NEW YORK MED COLL,DEPT BIOCHEM & MOLEC BIOL,VALHALLA,NY 10595

[5] NEW YORK MED COLL,DEPT MICROBIOL & IMMUNOL,VALHALLA,NY 10595

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 187卷 / 02期

关键词：

D O I：

10.1016/0006-291X(92)91260-W

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：

3α-Hydroxysteroid dehydrogenase is a cytosolic, monomeric, NADPH-dependent oxidoreductase which reduces 3-keto-5-dihydrosteroids to their tetrahydro products. We present here the first partial amino acid sequence data for the human liver enzyme and show these sequences to be identical to the deduced amino acid sequence for human hepatic chlordecone reductase. In addition, these two enzymes exhibit similar substrate and cofactor specificities and immunological reactivity. The results suggest that the natural substrates for chlordecone reductase are 3-keto-5-dihydrosteroids and that these two proteins may be identical. © 1992.

引用

页码：760 / 766

页数：7

共 28 条

[1] PREPARATIVE PURIFICATION OF HOMOGENEOUS STEROID-ACTIVE ISOENZYME OF HORSE LIVER ALCOHOL-DEHYDROGENASE BY AFFINITY CHROMATOGRAPHY ON AN IMMOBILIZED AMP-ANALOG [J].