Martin P M, Cochet C, Rolland P H, Chambaz E M
C R Acad Hebd Seances Acad Sci D. 1977 Apr 4;284(14):1305-7.
Evidence is presented demonstrating the presence of a high affinity (Ka10(8)M-1), limited capacity (3-4 pmoles/mg protein) estradiol binder in the soluble fraction of the Bovine, Rat and Human adrenal cortex. The binding appears specific to the estrogen structure whereas C19 and C21 steroids do not bind. Upon sucrose density gradient centrifugation, the estradiol binder sedimented at 9 S at low ionic strength and was shifted to 4.5 S in the presence of 0.5 M KCl. This demonstration of a receptor-like moiety for estradiol in the adrenal cortex lends biochemical support to previous observations suggesting that adrenal cortex functions may be modulated by a direct effect of gonadal steroid hormones.
有证据表明,在牛、大鼠和人类肾上腺皮质的可溶部分中存在一种高亲和力(Ka 10(8)M-1)、有限容量(3-4皮摩尔/毫克蛋白质)的雌二醇结合剂。这种结合似乎对雌激素结构具有特异性,而C19和C21类固醇则不结合。在蔗糖密度梯度离心时,雌二醇结合剂在低离子强度下以9 S沉降,在0.5 M KCl存在下则移至4.5 S。肾上腺皮质中存在类似雌激素受体部分的这一证明为先前的观察提供了生化支持,表明性腺甾体激素的直接作用可能调节肾上腺皮质功能。