Abstract
IN recent experiments in this laboratory, a substance has been demonstrated in human aortæ which is capable of coagulating fibrinogen independently of thrombin1. This factor, vasculokinase, appears to have no esterase, amidase or gelatinase activity. Nevertheless, its capability of catalysing fibrinogen to fibrin suggests that it may be a proteolytic enzyme. In previous experiments by Lorand and Middlebrook2, it has been shown that the N-terminal amino-acids of the fibrin monomer catalysed by thrombin are tyrosine and glycine. It has been suggested that there is a specific peptide site in the fibrinogen molecule which must be split in order for the monomers to polymerize3–4.
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MURRAY, M., GRAY, L. Terminal Amino-Acid Analysis of Vasculokinase-activated Fibrin. Nature 194, 681 (1962). https://doi.org/10.1038/194681a0
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DOI: https://doi.org/10.1038/194681a0
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