Abstract
IN addition to the abundant literature on plasmin inhibitors occurring in blood there are a few reports of an extractable tissue inhibitor of fibrinolysis1–3. It was during the course of an investigation commenced to further the characterization of the tissue inhibitor that a number of observations were made which led us to a reconsideration of the enzyme fibrinase. This enzyme occurs in blood and has been identified with the ‘Laki–Lorand factor’4 and ‘fibrin-stabilizing factor’5 by Loewy et al., who investigated a number of its properties6–9. The primary action of fibrinase is, in the presence of calcium, to convert a urea-soluble fibrin (fibrin s) to a urea-insoluble gel (fibrin i). Acetic acid (2 per cent v/v) or monochloracetic acid (1 per cent w/v) have similar solvent properties to 8 M urea in this respect.
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TYLER, H., LACK, C. A Tissue Fibrin-stabilizing Factor and Fibrinolytic Inhibition. Nature 202, 1114–1115 (1964). https://doi.org/10.1038/2021114a0
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DOI: https://doi.org/10.1038/2021114a0
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