Summary
A steroid sulphotransferase from human liver, catalysing the formation of dehydroepiandrosterone sulphate, was purified 10–12 fold by the following procedures: differential centrifugation, 30–50% saturation of the 150000 × g supernatant with ammonium sulphate, adsorption and elution from calcium phosphate-gel, chromatography on DEAE cellulose, gel nitration through Sephadex G-200. The K m -value for dehydroepiandrosterone was found to be 5 × 10-6 M, and the pH optimum ranges from 7,0–8,2 in Tris maleate buffer. Within 24 hr at + 5° the enzyme lost more than 50% of its initial activity.
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Gugler, R., Breuer, H. (1969). Isolierung einer Steroid-Sulfotransferase aus der Leber des Menschen. In: Kracht, J. (eds) Oestrogene Hypophysentumoren. Oestrogene Hypophysentumoren, vol 15. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-95126-8_34
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DOI: https://doi.org/10.1007/978-3-642-95126-8_34
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