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Purification of steroid sulphohydrolase from human placenta microsomes

Gniot-Szulzycka, J.; Januszewska, B.

Acta Biochimica Polonica 33(3): 203-215

1986

ISSN/ISBN: 0001-527X
PMID: 3468710
Document Number: 282501
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 .times. 10-5 M, specific activity 1563 nmol .cntdot. min-1 .cntdot. mg protein-1) from arylsulphatase C (Mr 45 000, optimum pH 7.6, Km 0.96 .times. 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.

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