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A proteinase, named BmooMPα-I, from the venom of Bothrops moojeni, was purified by DEAE-Sephacel, Sephadex G-75 and heparin-agarose column chromatography. The enzyme was purified to homogeneity as judged by its migration profile in SDS–PAGE stained with coomassie blue, and showed a molecular mass of about 24.5kDa. Its complete cDNA was obtained by RT-PCR and the 615bp codified for a mature protein...
Local and systemic hemorrhages are major problems concerning bites by viper snakes. Therefore, accessing venom hemorrhagic activity is an important feature in order to characterize viper venom major toxicities or to assay antivenom efficacy. The methods currently used to access hemorrhagic activity involve animal experiments and according to the general ethical committees, these procedures should...
Bleeding at the site of bite and/or systemic hemorrhage are symptoms frequently observed in envenomation by Bothrops jararaca snakes. In this study, we purified and characterized a prothrombin activator from B. jararaca that is probably involved in these clinical manifestations. The enzyme was isolated by a combination of gel filtration and ion exchange chromatographies and named bothrojaractivase...
Two activators of coagulation factor X, 58kDa VAFXA-I and 70kDa VAFXA-II, were purified from the venom of long-nosed viper (Vipera ammodytes ammodytes) by chromatography on gel filtration, affinity, ion-exchange and hydroxyapatite media. Both enzymes are glycoproteins composed of a heavy chain and two C-type lectin-like light chains all joined by disulphide bonds. LC–MS and LC–MS/MS analysis of their...
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