Brooks S C, Battelli M G, Corombos J D
J Steroid Biochem. 1987 Feb;26(2):285-90. doi: 10.1016/0022-4731(87)90084-7.
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 electrophoresis. The active protein displayed a pI of 6.1, pH optimum of 7.6-7.8 and a requirement of 10 mM Mg2+ for maximum transfer of sulfate from 3'-phosphoadenosine-5'-phosphosulfate (PAPS) to estrone (E1). Km of the reaction was 24 +/- 4.7 microM 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.
猪子宫内膜雌激素磺基转移酶已被分离并对其性质进行了研究。这种酶仅出现在经雌激素预处理并用孕酮处理的去卵巢小母猪的子宫中。通过对分泌期子宫内膜100,000g上清液进行色谱聚焦获得了该酶最稳定的形式。通过分子筛（Sephadex G-200 Superfine）和圆盘凝胶电泳测定该磺基转移酶的分子量为31 kDa。活性蛋白的pI为6.1，最适pH为7.6 - 7.8，将硫酸根从3'-磷酸腺苷-5'-磷酸硫酸酯（PAPS）最大程度转移至雌酮（E1）需要10 mM Mg2+。以PAPS为底物时反应的Km为24±4.7μM，以E1为底物时为24±9.8 nM。因此，猪子宫内膜磺基转移酶对E1的亲和力比先前从牛肾上腺中分离出的类似酶高得多。正如在其他组织的磺基转移酶中所观察到的那样，在整个纯化过程中，一种内源性底物（推测为E1）始终伴随着该酶。
