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Updated: Aug 9, 2026

Characterization of Leukocyte-platelet Rich Fibrin, A Novel Biomaterial
Published on: September 29, 2015
A low molecular weight urokinase derivative with enhanced fibrin affinity
Abstract:
A Gly-Pro-Arg-Pro tetrapeptide, homologous to amino-terminal segment of the human fibrin alpha chain after the release of the fibrinopeptide A, was covalently coupled to peptide A of low molecular weight urokinase. The resulting derivative gained increased affinity for fibrin. In caseinolytic assay, fibrin can stimulate the derivative to activate plasminogen. The derivative had two-fold greater fibrinolytic potency than native low molecular weight urokinase and its affinity for fibrin clot was 3.9-fold higher than that of low molecular weight urokinase.
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