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- W4240651421 abstract "The α2-plasmin inhibitor in plasma exists in at least two molecular forms (1). One form (PB) binds to plasminogen-Sepharose. The other form (NPB) comprising around 0.4 of the total amount of the inhibitor in plasma does not bind to plasminogen-Sepharose. PB was purified by affinity chromatography (1) while NPB was partially purified by conventional methods (2). Both inhibitor forms inhibited plasmin in a fast reaction and the change in catalytic concentration of plasmin with increasing concentrations of both forms was a linear function. At identical active site concentrations of the two forms (titrated with pNPGB-titrated plasmin) PB produced a more marked inhibition of urokinase-induced fibrinolysis. Similarily PB produced a more marked decrease of the binding af Lys-plasminogen to fibrin than NPB. The results indicate that an equilibrium between the 2 forms may be important for the biological regulation of the inhibition of plasmin. 1: I. Clemmensen, The Physiological Inhibitors of Coagulation and Fibrinolysis; D. Collen, B. Wiman, M. Verstraete, eds., p. 131-136, Amsterdam 1978. 2: U.Christansen & I. Clemmensen, Biochem. J., 175:635-641, 1978." @default.
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- W4240651421 date "1979-01-01" @default.
- W4240651421 modified "2023-10-18" @default.
- W4240651421 title "Functional Properties of Two Different Molecular Forms of α2-Plasmin Inhibitor" @default.
- W4240651421 doi "https://doi.org/10.1055/s-0039-1684510" @default.
- W4240651421 hasPublicationYear "1979" @default.
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