Stocker K, Fischer H, Meier J
Toxicon. 1982;20(1):265-73. doi: 10.1016/0041-0101(82)90225-2.
Proteinases affecting one or several physiological thrombin substrates are current components of Crotalidae and Viperidae venoms. Enzymes causing in vitro coagulation of fibrinogen without affecting other thrombin-susceptible blood constituents as well as enzymes affecting platelets, F. V. VIII and XIII with only minor action on fibrinogen have been isolated. Fibrinogen affecting proteinases may catalyze the release of either fibrinopeptide (Fp) A (e.g. ancrod, batroxobin) or Fp B (Agk, contortrix proteinase) or of both Fp A and B (B. gabonica proteinase). Some of these enzymes are inhibited by AT III-heparin complex (e.g. Agk. contortrix proteinase) some are not inhibited by either AT III-heparin or hirudin (e. g. batroxobin). The application of Fp A releasing venom proteinases into animals causes transformation of fibrinogen into fibrin I monomer which is rapidly degraded by fibrinolysis and thereby leads to a state of afibrinogenaemia. The administered enzyme is gradually bound to serum proteinase-inhibitors and inactivated. A species dependent interaction between venom enzyme, fibrinogen and serum proteinase inhibitors creates specific differences in dose response relationship. Thus, batroxobin isolated from B. moojeni (HOGE) proved to be a superior defibrinogenating agent in man, as compared to the closely related enzyme isolated from B. atrox (L.). LD50 of B. atrox venom in previously batroxobin defibrinogenated mice is not significantly different as compared to normal animals, indicating an only minor role of batroxobin in Bothrops venom poisoning.
影响一种或几种生理性凝血酶底物的蛋白酶是蝰蛇科和眼镜蛇科蛇毒的现有成分。已分离出在体外使纤维蛋白原凝固但不影响其他凝血酶敏感血液成分的酶，以及对血小板、因子Ⅷ和ⅩⅢ有影响但对纤维蛋白原作用较小的酶。影响纤维蛋白原的蛋白酶可能催化纤维蛋白肽（Fp）A（如安克洛酶、巴曲酶）或Fp B（矛头蝮蛋白酶、猪鼻蛇蛋白酶）或Fp A和B两者（加蓬咝蝰蛋白酶）的释放。其中一些酶被抗凝血酶Ⅲ - 肝素复合物抑制（如矛头蝮蛋白酶、猪鼻蛇蛋白酶），一些则不受抗凝血酶Ⅲ - 肝素或水蛭素抑制（如巴曲酶）。将释放Fp A的蛇毒蛋白酶应用于动物会导致纤维蛋白原转化为纤维蛋白I单体，该单体迅速被纤维蛋白溶解降解，从而导致无纤维蛋白原血症状态。所施用的酶会逐渐与血清蛋白酶抑制剂结合并失活。蛇毒酶、纤维蛋白原和血清蛋白酶抑制剂之间的种属依赖性相互作用在剂量反应关系中产生了特定差异。因此，与从矛头蝮（L.）分离出的密切相关的酶相比，从莫氏矛头蝮（HOGE）分离出的巴曲酶被证明是一种更优的去纤维蛋白原剂。在先前用巴曲酶去纤维蛋白原的小鼠中，矛头蝮蛇毒的半数致死量与正常动物相比无显著差异，这表明巴曲酶在矛头蝮蛇毒中毒中作用较小。
