Nielsen C J, Vogel W M, Pratt W B
Cancer Res. 1977 Sep;37(9):3420-6.
We have examined the rates of inactivation of glucocorticoid receptors in cell-free preparations from several rat tissues. The t1/2 of inactivation of the glucocorticoid-binding ability of thymus, heart, and kidney cytosols (37,000 X g supernatants) ranges from 2 to 4 hr at 0 degrees, whereas that of liver is much slower (15 to 25 hr). The rate of inactivation of the glucocorticoid-binding capacity of soluble preparations from liver varies roughly according to the g force at which they have been centrifuged. The 100,000 X g supernatant. The ability of the particulate enzyme to inactivate glucocorticoid receptors at 0 degrees is not affected by protease inhibitors but is inhibited by fluoride and molybdate. The rapid inactivation of unbound glucocorticoid receptors that occurs in a high-speed (100,000 X g) supernatant preparation from rat liver at 25 degrees can be completely inhibited by molybdate. These observations suggest that the inactivation of glucocorticoid receptors observed in cell-free liver preparations in vitro is due to a nonproteolytic enzymatic function.
我们已经检测了几种大鼠组织的无细胞制剂中糖皮质激素受体的失活速率。胸腺、心脏和肾脏胞质溶胶（37,000×g 上清液）中糖皮质激素结合能力的失活半衰期在 0℃时为 2 至 4 小时，而肝脏的则慢得多（15 至 25 小时）。肝脏可溶性制剂中糖皮质激素结合能力的失活速率大致根据其离心时的重力而变化。100,000×g 上清液。颗粒酶在 0℃时使糖皮质激素受体失活的能力不受蛋白酶抑制剂的影响，但受氟化物和钼酸盐的抑制。在 25℃下大鼠肝脏高速（100,000×g）上清液制剂中发生的未结合糖皮质激素受体的快速失活可被钼酸盐完全抑制。这些观察结果表明，体外在无细胞肝脏制剂中观察到的糖皮质激素受体失活是由于一种非蛋白水解酶功能。
