Properties of fibrinogen degradation products produced by alpha- and beta- fibrinogenases of Trimeresurus mucrosquamatus snake venom.

C. Ouyang, C.-M. Teng and Y.-C. Chen. Properties of fibrinogen degradation products produced by α- and β-fibrinogenases of T. mucrosquamatus snake venom. Toxicon17, 121–126, 1979.—Human fibrinogen was digested by α- and β-fibrinogenases of T. mucrosquamatus snake venom. Fifty per cent of the unclottable fibrinogen was precipitable by protamine sulfate, while only 5% of these degradation products were soluble in trichloroacetic acid. α- and β-fibrinogenases were weak anticoagulants as measured by recalcification time and plasma prothrombin time. The fibrinogen degradation products produced by β-fibrinogenase could polymerize with normal fibrin monomer, but prolonged the reaction time of thrombin with fibrinogen. α-Fibrinogenase inhibited platelet aggregation induced by ADP, while β-fibrinogenase did not.