1962/11/01 by Russell F. Doolittle, Douglas M. Surgenor · 2 citations
Chemistry · Environmental Science · Medicine · #Biochemistry #Biology #Blood Coagulation and Thrombosis Mechanisms #Blood properties and coagulation #Chemistry #Coagulation #Endocrinology #Fibrinogen #Fibrinolysis #Fish <Actinopterygii> #Fish biology, ecology, and behavior #Hagfish #Internal medicine #Medicine #Platelet #Thrombin
paper · doi:10.1152/ajplegacy.1962.203.5.964
openalex publication_date 1962/11/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/26
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.