Abstract
THE formation of fibrin is a fundamental biological repair mechanism, but the fibrin has ultimately to be removed by fibrinolysis. This is accomplished by the proteolytic enzyme plasmin, which is converted from plasminogen, an inactive precursor in blood, by an activator. Astrup and Permin1 have demonstrated that the fibrinolytic activity of tissues is due to such an activator of plasminogen.
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References
Astrup, T., and Permin, P. M., Nature, 159, 681 (1947).
Todd, A. S., Nature, 181, 495 (1958).
Todd, A. S., J. path. Bact., 78, 281 (1959).
Kwaan, H. C., Fed. Proc., 25, 52 (1966).
Brakman, P., Fibrinolysis, a standardized fibrin plate method and a fibrinolytic assay of plasminogen, (Scheltema and Holkema, Amsterdam, 1967).
Noordhoek Hegt, V., and Brakman, P., Fourth int. Congr., on Thrombosis, and Haemostasis Abstract no. 422 (1973).
Sgouris, J. T., Inman, J. K., McCall, K. B., Hyndman, L. A., and Anderson, H. D., Vox Sang., 5, 357 (1960).
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HEGT, V., BRAKMAN, P. Histochemical study of an inhibitor of fibrinolysis in the human arterial wall. Nature 248, 75–76 (1974). https://doi.org/10.1038/248075a0
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DOI: https://doi.org/10.1038/248075a0
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