Cholesterol sulphate sulphohydrolase of human placenta lysosomal membrane |
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Authors: | Roszek Katarzyna Gniot-Szulzycka Jadwiga |
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Institution: | Nicolaus Copernicus University, Institute of General and Molecular Biology, Biochemistry Department, ul. Gagarina 7, 87-100 Toruń, Poland. |
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Abstract: | 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. |
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