Takada Y, Makino Y, Takada A
Thromb Res. 1985 Aug 1;39(3):289-96. doi: 10.1016/0049-3848(85)90224-5.
Two isozymes of a native form of human plasminogen (plg), Glu-plg I and II, were isolated. Glu-plg I or II was activated by urokinase (UK) or streptokinase (SK) in the presence of fibrinogen or fibrin. The activation of Glu-plg I was enhanced more than that of Glu-plg II in the presence of fibrin. Fibrin caused better activation of both Glu-plg I and II than fibrinogen. When fibrinolysis or fibrinogenolysis was measured, fibrin was degraded faster than fibrinogen after the activation of Glu-plg I and II by UK. These results suggest that the activation of Glu-plg I was enhanced more than that of Glu-plg II in the presence of fibrin or to less extent fibrinogen.
分离出了天然形式的人纤溶酶原（plg）的两种同工酶，即Glu-plg I和II。在纤维蛋白原或纤维蛋白存在的情况下，Glu-plg I或II可被尿激酶（UK）或链激酶（SK）激活。在纤维蛋白存在时，Glu-plg I的激活比Glu-plg II的激活增强得更多。与纤维蛋白原相比，纤维蛋白对Glu-plg I和II的激活效果更好。当检测纤维蛋白溶解或纤维蛋白原溶解时，在UK激活Glu-plg I和II后，纤维蛋白比纤维蛋白原降解得更快。这些结果表明，在纤维蛋白存在时或在较小程度上在纤维蛋白原存在时，Glu-plg I的激活比Glu-plg II的激活增强得更多。
