Abstract
WE have found that isonicotinic acid hydrazide, a widely used drug1, is a potent inhibitor of the crosslinking of fibrin. This reaction constitutes the terminal step in normal blood coagulation and proceeds by way of an enzyme catalysed transpeptidation by forming inter-fibrin γ-glutamyl-ε-lysine bonds2,3. Compounds which resemble the donor (amine) or the acceptor (carbonyl) side-chain functions of fibrin specifically inhibit the crosslinking reaction without, however, interfering with gel formation—that is, clotting time—itself.
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LORAND, L., JACOBSEN, A. Isonicotinic Acid Hydrazide as an Inhibitor of Transpeptidation: Relevance for Blood Coagulation. Nature 216, 508–509 (1967). https://doi.org/10.1038/216508b0
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DOI: https://doi.org/10.1038/216508b0