Purification of testosterone 5 alpha-reductase from human prostate by a four-step chromatographic procedure.

Abstract:

:Nuclear membrane bound testosterone 5 alpha-reductase solubilized in active form from human prostatic tissue by 0.5% n-octyl beta-D-glucopyranoside was purified by a four-step chromatographic procedure including DEAE-Trisacryl ion exchange, hydroxylapatite adsorption, testosterone-Sepharose affinity and Sepharose 4B gel filtration. A purification of approximately 30-fold was achieved judging from the increase in the specific enzymatic activity. We have purified the acidic pH-optimum 5 alpha-reductase type 2 isoenzyme. The apparent molecular weight of the purified enzyme was estimated as 42,000 by SDS-PAGE. At the same time we isolated a 38 kDa protein characterized by a real affinity for testosterone and by a possible association to the 5 alpha-reductase enzyme.

journal_name

Steroids

journal_title

Steroids

authors

Quemener E,Amet Y,di Stefano S,Fournier G,Floch HH,Abalain JH

doi

10.1016/0039-128x(94)90103-1

subject

Has Abstract

pub_date

1994-12-01 00:00:00

pages

712-8

issue

12

eissn

0039-128X

issn

1878-5867

pii

0039-128X(94)90103-1

journal_volume

59

pub_type

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