Barańczyk-Kuźma A, Szymczyk T
Department of Biochemistry, Warsaw Medical School, Poland.
Biochem Pharmacol. 1987 Oct 1;36(19):3141-6. doi: 10.1016/0006-2952(87)90624-1.
Phenol sulfotransferases (PST) from bovine lung and small intestine were purified about 1000-fold. PST from bovine small intestine, similarly as the bovine lung enzyme, catalyzes sulfation of only exogenous phenols. A single thermostable form of PST, active with high concentrations of phenol (Km = 1.43 mM) was found in the small intestine. The effect of divalent cations on the activity of the two phenol sulfotransferases was determined. The molecular weight of the native enzymes was estimated as about 69,000 and subunit molecular weight determined by sodium dodecyl sulfate gel electrophoresis as 35,000. In double immunodiffusion tests the bovine lung PST showed antigenic identity with the bovine small intestine enzyme but complete immunological incompatibility with rat liver sulfotransferase.
牛肺和小肠中的酚磺基转移酶（PST）被纯化了约1000倍。牛小肠中的PST与牛肺酶类似，仅催化外源性酚的硫酸化。在小肠中发现了一种单一的热稳定形式的PST，在高浓度酚（Km = 1.43 mM）下具有活性。测定了二价阳离子对两种酚磺基转移酶活性的影响。天然酶的分子量估计约为69,000，通过十二烷基硫酸钠凝胶电泳测定的亚基分子量为35,000。在双向免疫扩散试验中，牛肺PST与牛小肠酶显示出抗原同一性，但与大鼠肝脏磺基转移酶完全免疫不相容。
