The action of a fibrin-promoting enzyme isolated from the venom of A.c.contortrix was investigated. The ratio of fibrinopeptides A and B released was similar in isolated human and rat fibrinogen and human plasma, fibrinopeptide B always being released preferentially. However, no clotting occurred in rat plasma, and no fibrinopeptides were released even after prolonged incubation. The results suggest strong, fast-acting irreversible neutralization of the enzyme activity in rat plasma.
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http://dx.doi.org/10.1016/0041-0101(90)90103-e | DOI Listing |
Arch Microbiol
July 2022
Department of Animal Morphology and Physiology, Federal Rural of University of Pernambuco, Recife Pernambuco, Brazil.
Thrombosis is a hematological disorder characterized by the formation of intravascular thrombi, which contributes to the development of cardiovascular diseases. Fibrinolytic enzymes are proteases that promote the hydrolysis of fibrin, promoting the dissolution of thrombi, contributing to the maintenance of adequate blood flow. The characterization of new effective, safe and low-cost fibrinolytic agents is an important strategy for the prevention and treatment of thrombosis.
View Article and Find Full Text PDFThe action of a fibrin-promoting enzyme isolated from the venom of A.c.contortrix was investigated.
View Article and Find Full Text PDFBiochim Biophys Acta
January 1989
Institute of Hematology and Blood Transfusion, Prague, Czechoslovakia.
Fibrin clot-promoting enzyme preferentially releasing fibrinopeptide B from fibrinogen was isolated from the crude venom of Agkistrodon contortrix and its mode of action was studied in detail. A purification procedure involving affinity chromatographies on immobilized lectin and arginine removed plasmin-like and kallikrein-like activities towards low-molecular-weight chromogenic substrates. Fibrin-promoting enzyme cleaved off only fibrinopeptides A and B from fibrinogen.
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