Tashima Y, Terui M, Itoh H, Mizunuma H, Kobayashi R, Marumo F
Department of Biochemistry, School of Medicine, Akita University.
J Biochem. 1989 Mar;105(3):358-61. doi: 10.1093/oxfordjournals.jbchem.a122668.
Rat liver glucocorticoid receptor was partially purified and characterized for its hormone binding using selenite. Selenite at very low concentrations irreversibly inhibited the hormone binding. The concentration for half maximal inhibition was approximately 2.8 microM. The inhibition was restored by dithiothreitol. The receptor-hormone complex became considerably insensitive to the selenite inhibition. The receptor inhibited by selenite was eluted at the same position as the native receptor from DEAE ion exchange and gel filtration columns. The results suggest that at least four sulfhydryl groups are located in the hormone binding domain of the receptor making a cluster.
利用亚硒酸盐对大鼠肝脏糖皮质激素受体进行了部分纯化，并对其激素结合特性进行了表征。极低浓度的亚硒酸盐可不可逆地抑制激素结合。半数最大抑制浓度约为2.8微摩尔。二硫苏糖醇可恢复这种抑制作用。受体 - 激素复合物对亚硒酸盐抑制作用变得相当不敏感。被亚硒酸盐抑制的受体与天然受体在DEAE离子交换柱和凝胶过滤柱上于相同位置洗脱。结果表明，至少四个巯基位于受体的激素结合结构域中形成一个簇。
