Overturf M L, Druihet R E, Fitz A
J Biol Chem. 1979 Dec 10;254(23):12078-83.
Pretreatment of hog high molecular weight renin for 30 min at 37 degrees C with 0.12 unit of either kallikrein or thrombin significantly increased (p less than 0.001) the amount of angiotensin I formed during subsequent incubations with homologous angiotensinogen. However, the thrombin-treated hog renin had 13 times more activity than the kallikrein-treated enzyme. Aprotinin did not inhibit the kallikrein-mediated activation of renin; the results indicated that aprotinin inhibited renin preferentially. Plasmin (0.25 unit) had little effect on the activity of high molecular weight renin. The molecular weight of hog renin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was not altered after exposure to either kallikrein, thrombin, or plasmin. These results do not exclude the occurrence of a limited proteolytic event or a conformational change beyond the detection of the current method. The data show that the activation of hog high molecular weight renin by thrombin and kallikrein was not associated with the conversion of renin to Mr = 43,000.
将猪高分子量肾素在37℃下用0.12单位的激肽释放酶或凝血酶预处理30分钟，在随后与同源血管紧张素原孵育期间，显著增加了（p < 0.001）生成的血管紧张素I的量。然而，经凝血酶处理的猪肾素的活性比经激肽释放酶处理的酶高13倍。抑肽酶不抑制激肽释放酶介导的肾素激活；结果表明抑肽酶优先抑制肾素。纤溶酶（0.25单位）对高分子量肾素的活性影响很小。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上，猪肾素暴露于激肽释放酶、凝血酶或纤溶酶后，其分子量没有改变。这些结果并不排除发生有限的蛋白水解事件或超出当前方法检测范围的构象变化。数据表明，凝血酶和激肽释放酶对猪高分子量肾素的激活与肾素转化为Mr = 43,000无关。
