Two forms of cholesterol sulfotransferase (CST) from rat epidermis

Document Type

Article

Publication Title

FASEB Journal

Abstract

Epidermis is an important site of cholesterol sulfation and the activity of the enzyme CST increases dramatically on squamous differentiation of human epidermal keratinocytes in culture(J. Invest. Dermatol. 93:108-115,1989). CSTfromrat epidermis has been partially purified by a combination of chromatography steps including hydrophobic interaction, ion exchange, gel filtration and chromatofocusing. A final purification step upon high resolution anion exchange chomatography (Resource QTM, Pharmacia) results in separation of two forms of the enzyme which presumably differ in their charge. Each form gives a major band of 40 kDa upon SDS-polyacrylamide gel electrophoresis. Despite the fact that a two- to four-fold difference in specific activity is observed between the two forms, no difference in Km and Vmax with respect to cholesterol is observed. A working hypothesis is that rat epidermal CST may form homo- and heterodimers in analogy with other sulfotransferases (J. Biol. Chem. 270:18941 -947,1995).

Publication Date

12-1-1996

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