The activation of two isozymes of glu-plasminogen (I and II) by urokinase and streptokinase.
Glu-plasminogen (Glu-plg) was eluted through lysine-Sepharose by using a gradient of 6 aminohexanoic acid, and two peaks corresponding to Glu-plg I and II were obtained. Glu-plg I has a molecular weight of 93,000 and Glu-plg II has a molecular weight of 89,000. When these plgs were activated by urokinase (UK) or streptokinase (SK) in the presence of S-2251 (H-D-Val-Leu-Lys-pNA0, the hydrolysis of S-2251 by Glu-plg I activated by UK or SK was larger than that by Glu-plg II activated by UK or SK. The results of SDS-PAGE indicate that the conversion of Glu-plg I to plasmin by UK was faster than that of Glu-plg II. It may be concluded that Glu-plg I is activated better to plasmin by activators than Glu-plg II.
D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000494:pharmacology*; D004789:Enzyme Activation; D007527:Isoenzymes / Q000032:analysis*; D010958:Plasminogen / Q000032:analysis* / Q000378:metabolism; D013300:Streptokinase / Q000494:pharmacology*; D014568:Urokinase-Type Plasminogen Activator / Q000494:pharmacology*
D007527:Isoenzymes; D010958:Plasminogen; D010450:Endopeptidases; D013300:Streptokinase; D014568:Urokinase-Type Plasminogen Activator