Steroid sulfotransferase in hamster epididymis |
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| Authors: | M Bouthillier A Chapdelaine G Bleau KD Roberts |
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| Institution: | Departments of Biochemistry and of Medicine University of Montreal and Maisonneuve-Rosemont Hospital Research Center Montreal, Canada |
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| Abstract: | Steroid sulfotransferase activity is present in the cytosol fraction of hamster epididymis. The activity of this enzyme is increased by magnesium ion. Cysteine is essential to assure optimal activity. Adenosine-3′-phosphate-5′-phosphosulfate is required as sulfate donor and an apparent Km of 62 μM was calculated. Inhibition studies suggest that this enzyme preferentially catalyzes the sulfurylation of the 3β-hydroxyl group of Δ5-steroids. An unusual feature of the enzyme is a pH optimum at pH 10. |
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