Purification of steroid sulphohydrolase from human placenta microsomes.
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.
Gniot-Szulzycka
J
J
Januszewska
B
B
D002845:Chromatography; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology*; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D043266:Steryl-Sulfatase; D013429:Sulfatases / Q000302:isolation & purification* / Q000378:metabolism
D013429:Sulfatases; D043266:Steryl-Sulfatase