Abstract
When Glu-plasminogen (Glu-plg) was incubated with urokinase (UK) in the presence of various concentrations of tranexamic acid and S-2251, the hydrolysis of S-2251 increased in the presence of 1 mM of tranexamic acid, but decreased in the presence of more than 10 mM of tranexamic acid. Use of SDS-polyacrylamide gel electrophoresis indicated: 1) Glu-plg was converted to plasmin better in the presence of 1 mM of tranexamic acid, but in the presence of more than 10 mM of tranexamic acid it was less converted. 2) Plg I (of higher molecular weight) was more easily converted than plg II by UK, but binding of tranexamic acid with lysine binding sites of plasminogen caused almost equal rate of activation of plg I and II.
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