Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom

Leiva, Laura; Maruñak, Silvana; Teibler, Pamela; Pérez, O. Acosta de

doi:10.1016/j.toxicon.2005.06.019

Cited by 57 publications

(49 citation statements)

References 29 publications

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“…Based on literature findings, we are able to assume that B. alternatus venom exhibits a variety of phospholipase A 2 and protease enzymes in its composition (30)(31)(32)(33)(34)(35)(36)(37)(38). At initial extraction steps all protein fractions are present in the system and each enzyme isoform is distributed between the phases, according to its structural properties.…”

Section: Resultsmentioning

confidence: 99%

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An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems

Gomez¹,

Nerli²,

Acosta³

et al. 2012

J. Venom. Anim. Toxins incl. Trop. Dis

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Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A 2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A 2 specific activities evidence the homogeneity of the isolated proteins.

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Section: Resultsmentioning

confidence: 99%

“…The whole venom shows three peak bands, a wide band that comprises proteins of molecular mass 50-60 kDa compatible with proteinases (59 kDa) and two closely placed bands of intermediate molecular mass (25 and 28 kDa respectivey) assignable to phospholipases A 2 and serine proteases (30,31).…”

Section: Resultsmentioning

confidence: 99%

An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems

Gomez¹,

Nerli²,

Acosta³

et al. 2012

J. Venom. Anim. Toxins incl. Trop. Dis

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“…This hemorrhagic metalloproteinases have myotoxic activities (28). Other hemorrhagic factors have been derived from different venoms (29)(30)(31). Their effects mechanisms have however been less discussed.…”

Section: Discussionmentioning

confidence: 99%

Properties of biological and biochemical effects of the Iranian saw-scaled viper (Echis carinatus) venom

Babaie¹,

Salmanizadeh²,

Zolfagharian³

et al. 2014

BLL

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Abstract:The venom of Echis carinatus is rich in proteins and peptides effective on the hemostatic system. This venom is contains metalloproteinase which convert prothrombin to meizothrombin. The prothrombin activator which leads to the formation of small blood clots inside the blood vessels throughout the body. To understand the mechanism of the effects of Iranian Echis carinatus venom, the effects of E. carinatus on human and Wistar rat plasma, plasma proteins (prothrombin and fi brinogen) and blood coagulation were studied. Proteolytic activity of the crude venom on blood coagulation factors such as prothrombin, partial thromboplastin and fi brinogen times were studied. In the present study the PT test for human plasma was reduced from 13.4 s (± 0.59) to 8.6 s (± 0.64) when human plasma was treated with crude venom (concentration of venom was 1 mg/ml) and for rat plasma PT was reduced from 14.5 s (± 0.47) to 8 s (± 0.49). Some possible biological and biochemical effects of IEc crude venom were investigated. The blood coagulation in human and in rat were investigated in vivo and in-vitro. In this paper, we show that the procoagulant action of Echis carinatus venom is due in part to a protein component that activates prothrombin and the procoagulant activity on human and rat plasma was evaluated (Tab. 2, Fig. 2, Ref. 31). Text in PDF www.elis.sk.

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“…Although venomics studies have revealed that metalloproteinases and serine proteinases are considered the most toxic components , we found that B. alternatus venom showed only moderate proteolytic activity. Souza et al (2000) found that B. alternatus venom contains a 55 kDa metalloproteinase, designated alternagin (Souza et al, 2000), which has been shown to be the major component responsible for the hemorrhagic effect of this venom, despite the fact that it displayed low proteolytic activity on casein (Gay et al, 2005). This could explain the moderate activity shown in the liquid assay and the absence of activity on the zymogram.…”

Section: Discussionmentioning

confidence: 99%

In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms

Campos

Pucca

Roncolato

et al. 2013

Toxicon

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In various types of snake venom, the major toxic components are proteinases and members of the phospholipase A2 family, although other enzymes also contribute to the toxicity. In this study, we evaluated the proteolytic, phospholipase, and L-Amino acid oxidase activities in the venom of five Bothrops species-Bothrops jararaca, Bothrops jararacussu, Bothrops moojeni, Bothrops neuwiedi, and Bothrops alternatus-all of which are used in the production of commercial antivenom, prepared in horses. The enzymatic activities of each species' venom were classified as high, moderate, or low. B. moojeni venom demonstrated the highest enzymatic activity profile, followed by the venom of B. neuwiedi, B. jararacussu, B. jararaca, and B. alternatus. To our knowledge, this is the first study to compare all of these enzymes from multiple species, which is significant in view of the activity of L-amino acid oxidase across Bothrops species.

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Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom

Cited by 57 publications

References 29 publications

An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems

An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems

Properties of biological and biochemical effects of the Iranian saw-scaled viper (Echis carinatus) venom

In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms

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