| Abstract: | The compositions of the proteolytic complexes of the venoms of the crotalid Agkistrodon halys halysand the viperid Echis multisquamatushave been investigated with the aid of a large number of specific natural and model substrates. A comparative analysis of the results obtained has revealed a predominance in the crotalid venom of fibrinogen-hydrolyzing enzymes, while the viperid venom is characterized as a procoagulant of the prothrombin-activating type. Among the fibrinogenases of the crotalid venom, a thrombin-like enzyme and a plasmin-like proteinase have been revealed and obtained in a purified state. A prothrombin-activating enzyme from the viperid venom has been isolated in the purified state and characterized with the aid of specific substrates.
Work performed with the support of the Nederlandse Organisatie voor Wetenschappelijk Onderzoek.Institute of Biochemistry of the Academy of Sciences of the Uzebekistan Republic, Tashkent. Department of Biochemistry, Cardiovascular Research Institute, University of Limburg, Maastricht, The Netherlands. Translated from Khimiya Prirodnykh Soedinenii, Vol. 3, pp. 447–454, May–June, 1993. |
