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人胎盘微粒体中硫酸胆固醇硫酸酯水解酶的亚基

Subunits of sterol sulphate sulphohydrolase from human placenta microsomes.

作者信息

Gniot-Szulzycka J, Wojczuk B

机构信息

Department of Biochemistry, Mikołaj Kopernik University, Toruń, Poland.

出版信息

J Steroid Biochem Mol Biol. 1992 Feb;41(2):141-3. doi: 10.1016/0960-0760(92)90040-p.

DOI:10.1016/0960-0760(92)90040-p
PMID:1543681
Abstract

A procedure for separation of the catalytic and regulatory subunits of sterol sulphate sulphohydrolase from human placenta microsomes with the use of Concanavalin A-Sepharose chromatography is presented. The Km value for the catalytic subunit with oestrone sulphate is 1.2 x 10(-5) M. The Hill coefficient value h, for the reconstituted enzyme complex is 3, the S0.5 = 0.68 x 10(-3) M and the value of Km is 0.31 x 10(-12) M. The regulatory subunit is trypsin sensitive, while the catalytic one is resistant to trypsin digestion.

摘要

介绍了一种利用伴刀豆球蛋白A-琼脂糖凝胶柱色谱法从人胎盘微粒体中分离硫酸酯硫酸水解酶催化亚基和调节亚基的方法。催化亚基对硫酸雌酮的米氏常数(Km)值为1.2×10⁻⁵M。重组酶复合物的希尔系数(h)值为3,半最大效应浓度(S0.5)=0.68×10⁻³M,米氏常数(Km)值为0.31×10⁻¹²M。调节亚基对胰蛋白酶敏感,而催化亚基对胰蛋白酶消化具有抗性。

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