Morris B J, Lawrence C H, Catanzaro D F
Clin Exp Pharmacol Physiol. 1980 Sep-Oct;7(5):563-7. doi: 10.1111/j.1440-1681.1980.tb00112.x.
The activation of inactive renin during incubation of human plasma with puff adder venom at pH 7.4 was found to be a complex process. Gel filtration on Sephacryl S-200 indicated that the venom contains a major peak of caseinolytic and renin-activating activity of low molecular weight. This enzyme was a metalloproteinase. During incubation with plasma the metalloproteinase formed a complex with alpha 2-macroglobulin and retained caseinolytic and reninactivation activity. Venom metalloproteinase activated prekallikrein, but not plasmin, and plasms kallikrein may account for at least part of the activation of inactive renin observed.
发现在pH 7.4条件下，人血浆与鼓腹咝蝰毒液一起孵育时，无活性肾素的激活是一个复杂的过程。在Sephacryl S - 200上进行凝胶过滤表明，毒液含有一个低分子量的酪蛋白水解和肾素激活活性的主要峰。这种酶是一种金属蛋白酶。在与血浆孵育过程中，金属蛋白酶与α2 -巨球蛋白形成复合物，并保留酪蛋白水解和肾素激活活性。毒液金属蛋白酶激活前激肽释放酶，但不激活纤溶酶，血浆激肽释放酶可能至少部分解释了所观察到的无活性肾素的激活。
