Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane.
In this paper we report that the activity of cholesterol sulphate sulphohydrolase (CHS-ase) is associated with the lysosomal membranes. The procedure of purification of CHS-ase from human placenta lysosomes was elaborated. The purified enzyme is highly specific to cholesterol sulphate (specific activity 2126.60+/-940.90 nmol min(-1) mg protein(-1)) and acts optimally at pH 3.4. The K(M) value for the hydrolysis of cholesterol sulphate is 3.6+/-0.95 x 10(-5)mol/l. The isoelectric point (pI) has the value 5.7, molecular weight estimated by SDS-PAGE electrophoresis is 38 kDa. The described enzyme may be involved in a regulation of cholesterol and cholesterol sulphate levels in the lysosomal membrane.
Roszek
Katarzyna
K
Nicolaus Copernicus University, Institute of General and Molecular Biology, Biochemistry Department, ul. Gagarina 7, 87-100 Toruń, Poland.
Gniot-Szulzycka
Jadwiga
J
D001192:Arylsulfatases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D005260:Female; D006801:Humans; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D051907:Lysosomal Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology*; D010920:Placenta / Q000201:enzymology*
D051907:Lysosomal Membrane Proteins; C466373:cholesterol sulfate sulfohydrolase; D001192:Arylsulfatases