Tseng L, Lee L Y, Mazella J
J Steroid Biochem. 1985 May;22(5):611-5. doi: 10.1016/0022-4731(85)90213-4.
Human placental estrogen sulfotransferase (ESFT) was partially purified from the term placental cytosol by (NH4)2SO4 precipitation and agarose gel chromatography. Additional purifications caused a rapid loss of the enzyme activity. The activity was abolished by isoelectrofocusing but partially retained by chromatofocusing. The value of pI of human placental ESFT is 5.8 and the same value was obtained for bovine adrenal ESFT. The enzyme protein was able to bind to the affinity resin, estradiol-17-hemisuccinyl-1,2-diaminododecane sepharose 4B, but difficult to be extracted by estradiol (E2). The extract of the affinity resin showed one major protein band at 68,000 dalton on SDS-polyacrylamide gel electrophoresis. Kinetic studies using partially purified ESFT revealed that E2 is the best substrate for this enzyme. The relative rate of sulfurylation of E2, estrone, estriol and dehydroepiandrosterone at 4 microM (Km for E2) is 1, 0.3, 0.08 and 0.08, respectively.
人胎盘雌激素磺基转移酶（ESFT）通过硫酸铵沉淀和琼脂糖凝胶色谱法从足月胎盘胞质溶胶中部分纯化。进一步纯化导致酶活性迅速丧失。等电聚焦使活性丧失，但色谱聚焦可部分保留活性。人胎盘ESFT的pI值为5.8，牛肾上腺ESFT也得到相同的值。酶蛋白能够与亲和树脂雌二醇-17-半琥珀酰-1,2-二氨基十二烷琼脂糖4B结合，但难以被雌二醇（E2）洗脱。亲和树脂提取物在SDS-聚丙烯酰胺凝胶电泳上显示一条主要的68,000道尔顿蛋白带。使用部分纯化的ESFT进行的动力学研究表明，E2是该酶的最佳底物。在4 microM（E2的Km值）下，E2、雌酮、雌三醇和脱氢表雄酮的硫酸化相对速率分别为1、0.3、0.08和0.08。
