Fibrinogenolytic activity of venom proteins of <em>Montivipera xanthina</em> (Gray, 1849) (Ophidia: Viperidae)
Keywords:Montivipera xanthina, tris-tricine SDS/PAGE, venom, Viperidae
In this study, with the aim of evaluating coagulant activities in the venom of Montivipera xanthina, we analyzed venom proteins, digestion patterns of fibrinogen chains incubated with venom, and the effects of protease inhibitors on M. xanthina venom proteases. Venom samples were obtained from four adult specimens collected in Gümüldür (Izmir, Turkey). SDS-PAGE analysis showed the presence of 17 protein bands or band groups in the molecular mass range of 20 to 200 kDa. The specific digestion patterns of fibrinogen chains revealed that M. xanthina venom possesses fibrinogenolytic enzymes, which could be involved in coagulation processes during envenomation. Fibrinogenolytic activity affected the Aα-chain and showed a time-dependent effect on Bβ-chains, which suggests the presence of both metalloproteinases and serine proteases in M. xanthina venom. After observing the fibrinogenolytic activity of M. xanthina venom, further research should focus on the isolation, identification, and characterization of individual venom components in order to provide insight into their function and biological roles
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