Abstract
A specific fibrinolytic agent was synthesized by covalently coupling urokinase to a monoclonal antibody that was fibrin-specific and did not cross-react with fibrinogen. The antibody was raised against a synthetic peptide representing the seven amino-terminal residues of the beta chain of human fibrin. The urokinase-antifibrin conjugate retained the original binding specificity of the antibody and showed 100-fold increased fibrinolysis in vitro when compared to unmodified urokinase. The presence of human fibrinogen at plasma concentration did not influence these properties.
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