Campbell P G, Pritchett J F, Marple D N, Till M L, Rahe C H
Steroids. 1982 Apr;39(4):445-52. doi: 10.1016/0039-128x(82)90068-x.
Glucocorticoid-binding activity in adrenal incubation media was investigated with regard to characterization of a protein-like ligand. Scatchard analysis of corticosterone binding activity indicated the presence of a single non-interacting protein with a dissociation constant (Kd) of 8.81 X 10(-10) M (0 degrees C), a value which is different from that of plasma and cytoplasmic glucocorticoid binding proteins. In addition, an observed lack of affinity of the protein for dexamethasone distinguishes the protein from Type II cytoplasmic receptor proteins. Thus our data suggest a glucocorticoid-binding protein which is distinct from the two known groups of glucocorticoid-binding proteins, corticosteroid-binding globulin (CBG) and cytoplasmic receptors.
关于一种蛋白质样配体的特性，对肾上腺孵育介质中的糖皮质激素结合活性进行了研究。对皮质酮结合活性的Scatchard分析表明存在一种单一的非相互作用蛋白，其解离常数（Kd）为8.81×10⁻¹⁰ M（0℃），该值与血浆和细胞质糖皮质激素结合蛋白的值不同。此外，观察到该蛋白对地塞米松缺乏亲和力，这使其与II型细胞质受体蛋白区分开来。因此，我们的数据表明存在一种糖皮质激素结合蛋白，它不同于已知的两类糖皮质激素结合蛋白，即皮质类固醇结合球蛋白（CBG）和细胞质受体。
