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以稳定且具有活性的形式对人前列腺5α-还原酶(3-氧代-5α-类固醇:NADP⁺ 4-烯氧化还原酶;EC 1.3.1.22)进行部分纯化。

Partial purification of human prostatic 5 alpha-reductase (3-oxo-5 alpha-steroid:NADP+ 4-ene-oxido-reductase; EC 1.3.1.22) in a stable and active form.

作者信息

Sargent N S, Habib F K

机构信息

University Department of Surgery (WGH), Western General Hospital, Edinburgh, Scotland.

出版信息

J Steroid Biochem Mol Biol. 1991 Jan;38(1):73-7. doi: 10.1016/0960-0760(91)90403-r.

DOI:10.1016/0960-0760(91)90403-r
PMID:1705142
Abstract

Human hyperplastic prostate tissue was homogenised in high ionic strength buffer and the post nuclear homogenate was incubated with 0.8% octyl glucoside and bovine brain lipids. Dialysis of the resulting liposome suspension yielded a preparation in which 5 alpha-reductase was active and stable for at least three weeks and showed an increase in specific activity (Vmax +/- SD = 48.9 +/- 7.4 pmol DHT/mg protein/ml) over that of the starting homogenate (Vmax +/- SD = 5.6 +/- 1.5 pmol DHT/mg protein/min) of 8.7 times.

摘要

将人增生性前列腺组织在高离子强度缓冲液中匀浆,然后将核后匀浆与0.8%辛基葡糖苷和牛脑脂质一起孵育。对所得脂质体悬浮液进行透析,得到一种制剂,其中5α-还原酶具有活性且至少三周内稳定,并且比起始匀浆(Vmax±SD = 5.6±1.5 pmol DHT/mg蛋白质/分钟)的比活性(Vmax±SD = 48.9±7.4 pmol DHT/mg蛋白质/毫升)提高了8.7倍。

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