Trial to analyse the substrate-multiplicity of plasmin by using a novel synthetic inhibitor
Abstract
Both the lysine binding site (LBS) and the active center of plasmin (P1) work together and result in the binding of Pl to its own substrate (fibrin) with extremely high selectivity. In the case of tranexamic acid (t-AMCHA), it binds only LBS, leaving the active center almost quite intact. Therefore, the active center is still able to cleave some oligopeptide-substrates as S-series even in the presence of lQ-2M of t-AMCHA. We report here a novel synthetic plasmin inhibitor called OS-153, chemically speaking, Na-{trans-[4-(aminomethyl)cyclohexyl] carbonyl}-L-lysine 4-benzoylanilide, which inhibits the function of the active center of Pl even at low concentration. Fact is, OS-153 inhibits not only the fibrinolysis (I5U=6.1saM) but amidolysis (Ki=7,4pM), Furthermore, OS-153 inhibits also "bradykinin forming activity" from the human intact plasma, which is activated by large-dose of strepto-
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