Gramse M, Egbring R, Havemann K
Hoppe Seylers Z Physiol Chem. 1984 Jan;365(1):19-26. doi: 10.1515/bchm2.1984.365.1.19.
Plasminogen-binding human alpha 2-plasmin inhibitor is converted by human granulocyte elastase into its non-plasminogen-binding and finally into the inactive form of the inhibitor. This degradation of the plasmin inhibitor, described earlier as "spontaneously" occurring conversion, is shown in dodecyl sulfate polyacrylamide gel electrophoresis, in two-dimensional immunoelectrophoresis and by measuring the kinetics of plasmin inhibition. Experiments in the presence of normal human plasma required unphysiologically high concentrations of elastase to inactivate alpha 2-plasmin inhibitor, suggesting a role of elastase in this type of indirect fibrinolysis in a microenvironment only and not in systemic events.
结合纤溶酶原的人α2 - 纤溶酶抑制剂被人粒细胞弹性蛋白酶转化为非结合纤溶酶原的形式，并最终转化为抑制剂的无活性形式。这种纤溶酶抑制剂的降解，先前被描述为“自发”发生的转化，在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳、二维免疫电泳以及通过测量纤溶酶抑制动力学中得到了体现。在正常人血浆存在的情况下进行的实验表明，需要非生理高浓度的弹性蛋白酶才能使α2 - 纤溶酶抑制剂失活，这表明弹性蛋白酶仅在微环境中这种间接纤维蛋白溶解类型中起作用，而在全身事件中不起作用。
