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Studies on a 3β3-hydroxysteroid sulphotransferase from rat liver

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Enzymology
0005-2744
Publisher
Elsevier
Publication Date
Volume
429
Issue
2
Identifiers
DOI: 10.1016/0005-2744(76)90287-4
Disciplines
  • Biology

Abstract

Abstract A steroid sulphotransferase (EC 2.8.2.2) was partially purified from female rat liver. The enzyme was active towards the substrates, dehydroepiandrosterone, epiandrosterone and pregnenolone but was inactive towards oestrogens, cholesterol and ergocalciferol. A pH optimum of 5.0 was recorded but the enzyme was unstable at low pH. The enzyme was stimulated slightly by the addition of reducing agents and inhibited by p- chloromercuribenzoate and HgCl 2. Crude enzyme activity was markedly stimulated by divalent cations but this effect was not observed with purified enzyme. A K m of 13 μM was calculated for the donor substrate 3′-phosphoadenylyl sulphate and the acceptor substrate, dehydroepiandrosterone had a K m value of 6 μM. The enzyme appeared to be highly susceptible to product inhibition by adenosine 3′,5′diphosphate.

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