Steroids p. 697 - 708 (1980)
Update date:2022-08-17
Topics:
Lin, Y. N.
Horowitz, M. I.
A sulfotransferase which catalyzes transfer of the sulfate group from 3'-phosphoadenosine-5'phosphosulfate to cholesterol has been demonstrated in the rat gastric mucosa.The product of the reaction was characterized as cholesterol sulfate by two-dimensional thin-layer chromatography behavior, and gas-liquid chromatography of cholesterol after acid solvolysis.The bulk of enzyme activity was found in the cytosol fraction.Sulfation of cholesterol did not require added Mg+2, Mn+2, or Ca+2, and was unaffected by ethylenediaminetetraacetate.Triton X-100 moderatly enhanced the enzyme activity.A broad pH optimum from pH 6.0 - 9.0 was exhibited with a maximum at pH 7.0 - 7.5.The apparent Km for PAPS was 0.8 x 10-6M.The possible function of cholesterol sulfate in gastric mucosa is discussed.
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