Wrange O
Biochim Biophys Acta. 1976 Jun 15;434(2):483-9. doi: 10.1016/0005-2795(76)90238-5.
Using a gel filtration on Sephadex G-150 in low ionic strength, it was possible to separate a corticosterone-binding protein in rat liver cytosol from corticosteroid-binding globulin after incubation of cytosol with [3H]corticosterone. The corticosterone-protein complex ("alpha-Complex") had a sedimentation coefficient of 8-9 S in low ionic strength. In high ionic strength, the alpha-Complex rapidly dissociated with a half-life of 15 h, compared to a half-life of 31 h for the hepatic dexamethasone-receptor complex under identical conditions (0 degrees C). The alpha-Compelx was saturable with an excess of unlabelled corticosterone of dexamethasone and was sensitive to heat and protease digestion. It is stressed that quantitation of the corticosterone-receptor complex must include separation of the receptor from corticosteroid-binding globulin as this protein binds corticosterone with high affinity and with a saturable amount of binding sites.
在低离子强度下使用葡聚糖凝胶G - 150进行凝胶过滤，在将大鼠肝细胞溶胶与[³H]皮质酮孵育后，有可能将肝细胞溶胶中的皮质酮结合蛋白与皮质类固醇结合球蛋白分离。在低离子强度下，皮质酮 - 蛋白质复合物（“α-复合物”）的沉降系数为8 - 9 S。在高离子强度下，α-复合物迅速解离，半衰期为15小时，而在相同条件（0℃）下，肝地塞米松受体复合物的半衰期为31小时。α-复合物可被过量的未标记皮质酮或地塞米松饱和，并且对热和蛋白酶消化敏感。需要强调的是，皮质酮受体复合物的定量必须包括将受体与皮质类固醇结合球蛋白分离，因为这种蛋白质以高亲和力和饱和数量的结合位点结合皮质酮。
