Yu P H, Rozdilsky B, Boulton A A
J Neurochem. 1985 Sep;45(3):836-43. doi: 10.1111/j.1471-4159.1985.tb04070.x.
An arylamine sulfotransferase (PST-M) from human brain cortex that is involved in the formation of O-sulfate esters of monoamines has been purified 272-fold by ammonium sulfate fractionation, gel filtration, DEAE-cellulose ion-exchange chromatography, chromatofocussing, and hydroxyapatite chromatography. A molecular weight of 62,000, pK of pH 5.8, and an optimum pH for the reaction at 7.8-8.0 with respect to tyramines have been determined. This enzyme possesses an extremely high affinity for dopamine and m-tyramine based on the low Km values and is moderately active toward noradrenaline and p-tyramine. Serotonin is a poor substrate. In contrast, another sulfotransferase, PST-P, which has been separated from PST-M and partially purified, exhibited a very high affinity for phenol and nitrophenols but was inactive toward the amine sulfate acceptors. In the human brain the specific activity toward dopamine as well as the ratio of activity toward dopamine/phenol was considerably higher than those for rat, hog, and bovine brains.
一种来自人类大脑皮层的芳胺磺基转移酶（PST-M）参与单胺O-硫酸酯的形成，通过硫酸铵分级分离、凝胶过滤、DEAE-纤维素离子交换色谱、聚焦色谱和羟基磷灰石色谱已将其纯化了272倍。已确定其分子量为62,000，pK为pH 5.8，相对于酪胺，反应的最适pH为7.8 - 8.0。基于低Km值，该酶对多巴胺和间酪胺具有极高的亲和力，对去甲肾上腺素和对酪胺有中等活性。血清素是一种较差的底物。相比之下，另一种已从PST-M中分离并部分纯化的磺基转移酶PST-P，对苯酚和硝基苯酚具有非常高的亲和力，但对胺硫酸盐受体无活性。在人类大脑中，对多巴胺的比活性以及多巴胺/苯酚的活性比显著高于大鼠、猪和牛的大脑。
