Blood coagulation in fish
- 1 November 1962
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Legacy Content
- Vol. 203 (5), 964-970
- https://doi.org/10.1152/ajplegacy.1962.203.5.964
Abstract
Blood coagulation systems in cyclostome, elasmobranch, and teleost fish were studied and compared. The plasma of all these fish contained a fibrinogen molecule, capable of being clotted by human thrombin, and a prothrombin molecule, capable of being converted into thrombin which could hydrolyze p-tosyl l-arginine methyl ester. The prothrombin activity could be adsorbed on barium sulfate. Accurate assessment of prothrombin conversion factors is confounded by the "species specificity" of protein-protein interactions, but preliminary observations were made on both the extrinsic and intrinsic clotting schemes. Fish thrombocytes play a central role in the intrinsic conversion of prothrombin to thrombin, and are responsible for clot retraction. The plasma of the smooth dogfish exemplifies a clotting diathesis which can be overcome in vitro by the addition of large amounts of calcium. Under such conditions, other parts of the coagulation scheme become greatly exaggerated, and a very large thrombin generation ensues, subsequently followed by an intense fibrinolysis. A powerful serum inhibition occurs which was shown to be caused by the breakdown products of the fibrinolysis.This publication has 5 references indexed in Scilit:
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