Electrophoretic Characterization of Venom Proteins of Montivipera xanthina (Gray, 1849) (Ophidia: Viperidae)

In this study, with the aim of evaluating coagulant activities in the venom of M. xanthina, we analyzed venom proteins, digestion patterns of fibrinogen chains with venom and the effects of protease inhibitors on M. xanthina venom proteases using Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis. Venom samples were obtained from four adult specimens of Montivipera xanthina collected in Gümüldür (Izmir, Turkey). SDS-PAGE analysis demonstrated that 17 protein bands in the range of 20–250 kDa were present. The specific digestion patterns of fibrinogen chains revealed that M. xanthina venom possesses fibrinogenolytic enzymes which could be included in coagulation processes during envenomation Fibrinogenolytic activity directed exclusively towards the Aa-chain with a time-dependent activity towards Bb-chains suggests the presence of both metalloproteinases and serine proteases in M. xanthine venom. In the present study, the occurrence and inhibition of fibrinogenolytic activity of M. xanthina venom were clearly observed. For further analysis, the isolation, identification, and characterization of individual venom components will provide insight into their function and biological roles.