从人胎盘微粒体中纯化类固醇硫酸酯酶

Purification of steroid sulphohydrolase from human placenta microsomes.

作者信息

Gniot-Szulzycka J, Januszewska B

出版信息

Acta Biochim Pol. 1986;33(3):203-15.

Abstract

A procedure for purification of oestrone sulphate sulphohydrolase from human placenta microsomes was elaborated. The use of Concanavalin-A-Sepharose chromatography made it possible to separate, for the first time, oestrone sulphate sulphohydrolase (Mr 36,000, optimum pH 7.0, Km 5.5 X 10(-5) M, specific activity 1563 nmol X min-1 X mg protein-1) from arylsulphatase C (Mr 45,000, optimum pH 7.6, Km 0.96 X 10(-3) M). The observed third subfraction showed both arylsulphate C and oestrone sulphate sulphohydrolase activity. Sigmoidal kinetics of oestrone sulphate sulphohydrolase after DEAE-cellulose chromatography (Mr 130,000) points to the allosteric character of the enzyme.

摘要

详细阐述了从人胎盘微粒体中纯化硫酸雌酮硫酸酯酶的方法。使用伴刀豆球蛋白A-琼脂糖凝胶层析首次实现了将硫酸雌酮硫酸酯酶（分子量36,000，最适pH 7.0，米氏常数5.5×10⁻⁵ M，比活性1563 nmol·min⁻¹·mg蛋白⁻¹）与芳基硫酸酯酶C（分子量45,000，最适pH 7.6，米氏常数0.96×10⁻³ M）分离。观察到的第三个亚组分同时具有芳基硫酸酯酶C和硫酸雌酮硫酸酯酶活性。硫酸雌酮硫酸酯酶经二乙氨基乙基纤维素层析后（分子量130,000）呈现S形动力学，表明该酶具有别构特性。