Denisov Iu P, Sergeev P V, Saksonov N P, Shutko G V
Biull Eksp Biol Med. 1980 Feb;89(2):172-4.
Parameters of cortisone and estradiol binding to plasmatic membranes of rat hepatocytes were studied by liquid scintillation radiometry. Two systems of binding these hormones were revealed in the membranes. One of the systems is specific (saturated) and binds the hormones in physiological concentrations. The capacity and affinity of this system for cortisone is significantly higher as compared to estradiol. The parameters of binding over the temperature range of 4-37 degrees C are as follows for cortisone and estradiol, respectively: dissociation constant 2.1-3 and 2.7-4.5 nM; the number of binding sites 2.0-2.4 and 0.14-0.18 nM per one g protein. Experiments with parachlormercuribenzoate indicate participation of proteins in this system functioning. The other (unsaturated) system is nonspecific, its funtioning being determined by the lipid component of the membranes. Corticosteroid affinity for hepatocytes seems likely to be due to the functioning of the specific (saturated) system of the plasmatic membranes of these cells.
采用液体闪烁辐射测量法研究了可的松和雌二醇与大鼠肝细胞质膜结合的参数。在膜中发现了两种结合这些激素的系统。其中一个系统是特异性的（饱和的），能在生理浓度下结合激素。与雌二醇相比，该系统对可的松的结合能力和亲和力显著更高。在4 - 37摄氏度温度范围内，可的松和雌二醇的结合参数分别如下：解离常数2.1 - 3和2.7 - 4.5 nM；每克蛋白质的结合位点数为2.0 - 2.4和0.14 - 0.18 nM。对氯汞苯甲酸实验表明蛋白质参与了该系统的功能。另一个（不饱和）系统是非特异性的，其功能由膜的脂质成分决定。皮质类固醇对肝细胞的亲和力可能归因于这些细胞质膜特异性（饱和）系统的功能。
