Purification of steroid sulphohydrolase from human placenta microsomes.

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.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Gniot-Szulzycka J,Januszewska B

subject

Has Abstract

pub_date

1986-01-01 00:00:00

pages

203-15

issue

3

eissn

0001-527X

issn

1734-154X

journal_volume

33

pub_type

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