Kress L F, Kurecki T
Biochim Biophys Acta. 1980 Jun 13;613(2):469-75. doi: 10.1016/0005-2744(80)90101-1.
Proteinase II from Crotalus adamanteus venom formed a complex with human alpha 2-macroglobulin in which approx. 1.7 mol of enzyme were bound per mol inhibitor. The complex did not enzymatically inactivate human alpha 1 proteinase inhibitor. However, active proteinase II was released from the complex in the presence of a high molecular weight proteinase fraction from C. adamanteus venom. The alpha 2-macroglobulin-proteinase II complex was also unstable during incubation in serum, and the enzyme released from the complex caused inactivation of serum proteinase inhibitors. The results indicate conditions under which venom proteinases can be dissociated from their complexes with alpha 2-macroglobulin and thus remain functional in the presence of molar excesses of inhibitor.
矛头蝮蛇毒中的蛋白酶II与人类α2-巨球蛋白形成了一种复合物,其中每摩尔抑制剂结合约1.7摩尔的酶。该复合物不会使人类α1蛋白酶抑制剂发生酶促失活。然而,在存在来自矛头蝮蛇毒的高分子量蛋白酶组分的情况下,活性蛋白酶II会从复合物中释放出来。α2-巨球蛋白-蛋白酶II复合物在血清中孵育时也不稳定,从复合物中释放出的酶会导致血清蛋白酶抑制剂失活。结果表明了毒液蛋白酶可以从它们与α2-巨球蛋白的复合物中解离的条件,从而在存在摩尔过量抑制剂的情况下仍保持功能。