人皮质类固醇结合球蛋白与细胞膜的特异性结合。
Specific binding of human corticosteroid-binding globulin to cell membranes.
作者信息
Hryb D J, Khan M S, Romas N A, Rosner W
出版信息
Proc Natl Acad Sci U S A. 1986 May;83(10):3253-6. doi: 10.1073/pnas.83.10.3253.
Abstract
Specific binding sites for corticosteroid-binding globulin were detected on membranes prepared from human prostates. The binding sites are typical of membrane receptors: they are saturable and specific and have high affinity. There was little specific binding at 4 degrees C and 23 degrees C. Maximal specific binding was obtained at 37 degrees C. Scatchard analysis revealed the presence of a single set of binding sites with an apparent dissociation constant of 8.7 X 10(-7) M and a binding capacity of 22 pmol/mg of membrane protein. The sites were specific for corticosteroid-binding globulin; binding was not inhibited by human testosterone/estradiol-binding globulin, by albumin, or by transferrin. The density of specific binding sites in membranes obtained from several organs from the rhesus monkey is consistent with the hypothesis that corticosteroid-binding globulin is involved in the transport of steroid hormones into target tissues.
摘要
在从人前列腺制备的膜上检测到了皮质类固醇结合球蛋白的特异性结合位点。这些结合位点具有膜受体的典型特征：它们是可饱和的、特异性的且具有高亲和力。在4℃和23℃时特异性结合很少。在37℃时获得最大特异性结合。Scatchard分析显示存在一组单一的结合位点，其表观解离常数为8.7×10⁻⁷M，结合容量为22 pmol/mg膜蛋白。这些位点对皮质类固醇结合球蛋白具有特异性；人睾酮/雌二醇结合球蛋白、白蛋白或转铁蛋白均不抑制结合。从恒河猴的多个器官获得的膜中特异性结合位点的密度与皮质类固醇结合球蛋白参与类固醇激素向靶组织转运的假说一致。
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