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- W2069371569 abstract "Porcine endometrial estrogen sulfotransferase has been isolated and its properties examined. This enzyme only appeared in uteri from ovariectomized gilts which had been primed with estrogen and treated with progesterone. The most stable form of the enzyme was obtained via chromatofocusing of the 100,000 g supernatant from secretory endometrium. A molecular weight of 31 KDa was determined for this sulfotransferase by molecular sieve (Sephadex G-200 Superfine) and disk-gel eleetrophoresis. The active protein displayed a pI of 6.1, pH optimum of 7.6–7.8 and a requirement of 10mM Mg2+ for maximum transfer of sulfate from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to estrone (E1). Kmof the reaction was 24 ± 4.7μM for PAPS and 24 ± 9.8 nM for E1 as substrate. Porcine endometrial sulfotransferase thus displayed a much greater affinity for E1 than a similar enzyme previously isolated from bovine adrenals. As has been observed of sulfotransferases from other tissues, an endogenous substrate (presumed to be E1) accompanies the enzyme throughout its purification." @default.
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- W2069371569 date "1987-02-01" @default.
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- W2069371569 title "Endocrine steroid sulfotransferases: Porcine endometrial estrogen sulfotransferase" @default.
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- W2069371569 doi "https://doi.org/10.1016/0022-4731(87)90084-7" @default.
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