Conversion of proteolytically modified form (Lys-form) of human plasminogen to plasmin by urokinase in the presence of tranexamic acid

Abstract

Proteolytically modified plasminogen (Lys-plg) was converted to plasmin by urokinase (UK) in the presence of various concentrations of tranexamic acid. Lys-plg was converted to plasmin faster by UK than a native form of plasminogen (Glu-plg). Both L-plg I and II were converted to plasmin in almost equal rate by UK in contrast to Glu-plg I and II , in which Glu-plg I was converted faster than Glu-plg II . Larger concentrations of tranexamic acid caused less conversion of L-plg, which may be due to competitive inhibition of UK by tranexamic acid. Heavy and light chains of Lys-plasmin were further degraded upon longer incubation.