PARTIAL-PURIFICATION OF 3-ALPHA-HYDROXYSTEROID AND 3-BETA-HYDROXYSTEROID DEHYDROGENASES FROM HUMAN HYPERPLASTIC PROSTATE - COMPARISON BETWEEN THE 2 ENZYMES

被引：7

作者：

AMET, Y ^{[1
]}

SIMON, B ^{[1
]}

QUEMENER, E ^{[1
]}

MANGIN, P ^{[1
]}

FLOCH, HH ^{[1
]}

ABALAIN, JH ^{[1
]}

机构：

[1] CHU MORVAN,SERV UROL,F-29200 BREST,FRANCE

来源：

JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1992年 / 41卷 / 3-8期

关键词：

D O I：

10.1016/0960-0760(92)90405-8

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：

3-alpha-Hydroxysteroid dehydrogenase (3-alpha-HSD) activity has been purified to homogeneity, the enzyme is a monomer with a M(w) of 32,000 Da. 3-beta-Hydroxysteroid dehydrogenase (3-beta-HSD) activity has been partially purified and has an apparent M(w) of 30,000 Da. Both enzymes have the same cofactor requirements, optimal pH. However 3-beta-HSD appeared to be an integral protein dependent on protein environment for its activity while 3-alpha-HSD activity is a protein more loosely associated to membranes.

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页码：689 / 692

页数：4

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