Kurokawa R, Hatakeyama S, Kyakumoto S, Ota M
Biochem Int. 1986 Oct;13(4):671-9.
Neoplastic epithelial duct cell line from human salivary gland (HSG cell) contained cytosol glucocorticoid receptor. Scatchard analysis of cytosol indicated that the dissociation constant (Kd) was 5.6-6.5 nmol/l and the number of binding sites was 83-92 fmol/mg protein. A competitive assay showed that the binding sites for [3H]triamcinolone acetonide were specific to glucocorticoid. Glycerol density gradient centrifugation displayed that the [3H]triamcinolone acetonide receptor complexes sedimented in the 8.5 S region under low salt conditions and in the 4.2 S region under high salt condition (0.4 M KCl). The same high salt conditions induced an increased binding of [3H]triamcinolone acetonide complexes for DNA-cellulose.
人唾液腺来源的肿瘤上皮导管细胞系(HSG细胞)含有胞质糖皮质激素受体。对胞质进行Scatchard分析表明,解离常数(Kd)为5.6 - 6.5 nmol/l,结合位点数量为83 - 92 fmol/mg蛋白。竞争性分析显示,[3H]曲安奈德结合位点对糖皮质激素具有特异性。甘油密度梯度离心显示,[3H]曲安奈德受体复合物在低盐条件下沉淀于8.5 S区域,在高盐条件(0.4 M KCl)下沉淀于4.2 S区域。相同的高盐条件导致[3H]曲安奈德复合物与DNA纤维素的结合增加。