McIlroy P J, Ryan R J
Endocrinology. 1983 Feb;112(2):476-81. doi: 10.1210/endo-112-2-476.
The effects of chymotrypsin on rat luteal adenylate cyclase have been investigated. Maximal stimulation occurred at a concentration of 10 micrograms/ml. This dose of chymotrypsin stimulated basal, GTP-,5'-(beta, gamma-imido)triphosphate-, and NaF-stimulated adenylate cyclase activity 2- to 3-fold. hCG-stimulated activities were stimulated 5- to 6-fold by the proteinase and showed a synergistic effect. The proteinase did not alter the hCG response curve, and the effect could not be mimicked by trypsin. Proteolytic activity was required, since chymotrypsinogen and inactivated chymotrypsin were not effective. The presence of chymotrypsin could not restore the hormonal sensitivity of a proteinase inhibitor-inactivated system. The results suggest that chymotrypsin stimulated rat luteal adenylate cyclase activity by two or more mechanisms: 1) a direct action on the catalytic subunit or a closely associated protein, and 2) an action somewhere in the pathway of hormonal stimulation.
已对胰凝乳蛋白酶对大鼠黄体腺苷酸环化酶的作用进行了研究。在浓度为10微克/毫升时出现最大刺激作用。该剂量的胰凝乳蛋白酶使基础的、GTP、5'-（β，γ-亚氨基）三磷酸和NaF刺激的腺苷酸环化酶活性提高了2至3倍。蛋白酶使hCG刺激的活性提高了5至6倍，并显示出协同作用。蛋白酶未改变hCG反应曲线，且胰蛋白酶无法模拟该作用。由于需要蛋白水解活性，因此胰蛋白酶原和失活的胰凝乳蛋白酶无效。胰凝乳蛋白酶的存在无法恢复蛋白酶抑制剂失活系统的激素敏感性。结果表明，胰凝乳蛋白酶通过两种或更多种机制刺激大鼠黄体腺苷酸环化酶活性：1）对催化亚基或紧密相关蛋白的直接作用，以及2）在激素刺激途径中的某个位置起作用。
