Glu-plasminogen I and II: their activation by urokinase and streptokinase in the presence of fibrin and fibrinogen.
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.
D000495:Allosteric Site; D004789:Enzyme Activation / Q000187:drug effects; D005337:Fibrin / Q000494:pharmacology; D005340:Fibrinogen / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D010958:Plasminogen / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D013300:Streptokinase / Q000494:pharmacology; D014568:Urokinase-Type Plasminogen Activator / Q000494:pharmacology
D005337:Fibrin; D005340:Fibrinogen; D010958:Plasminogen; D013300:Streptokinase; D014568:Urokinase-Type Plasminogen Activator