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dc.contributor.author
Gay, Claudia Carolina
dc.contributor.author
Leiva, Laura Cristina Ana
dc.contributor.author
Maruñak, Silvana
dc.contributor.author
Teibler, Gladys Pamela
dc.contributor.author
Acosta de Pérez, Ofelia
dc.date.available
2018-05-09T18:57:42Z
dc.date.issued
2005-10
dc.identifier.citation
Gay, Claudia Carolina; Leiva, Laura Cristina Ana; Maruñak, Silvana; Teibler, Gladys Pamela; Acosta de Pérez, Ofelia; Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom; Pergamon-Elsevier Science Ltd; Toxicon; 46; 5; 10-2005; 546-554
dc.identifier.issn
0041-0101
dc.identifier.uri
http://hdl.handle.net/11336/44666
dc.description.abstract
A hemorrhagic metalloproteinase has been isolated from Bothrops alternatus venom from specimens that inhabit the north-east region of Argentina. The present study aimed at evaluating the proteolytic, hemorrhagic, edematogenic and myotoxic activities of the purified metalloproteinase, in order to consider its participation on the phatophysiology of the intoxication by Bothrops alternatus venom. The hemorrhagic metalloproteinase was isolated by a combination of DEAE-Cellulose chromatography and gel filtration on Sephadex G-75. The enzyme showed a molecular mass around 55 kDa, it exhibited a hemorrhagic activity with a minimal hemorrhagic dose of 1.9 μg, almost two fold minor than the whole venom (3.6 μg). The enzyme showed a weak proteolytic activity on casein (18.72 U/mg enzyme), similar to the one exhibited by the whole venom (20 U/mg venom). Besides, the ability to degrade casein could be detected by SDS-PAGE; β-casein was the fraction that showed the higher degradation, followed by αs1-casein and κ-casein degradation. The hemorrhagic metalloproteinase rapidly hydrolysed the Aα-chain of fibrinogen, followed by Bβ-chain degradation and leaving the γ-chain unaffected. Proteolytic activities were inhibited by EDTA whereas they were not inhibited by benzamidine and PMSF. The metalloproteinase showed several polypeptides chains after autocatalytic processing, including a chain of 28 kDa, it could be the processed disintegrin-like and cysteine-rich domains. The isolated enzyme exhibited myotoxic activity with high CK levels at 6 h, due to local ischemia resulting of its hemorrhagic activity, and a significant edema-inducing effect (MED=1.3 μg), corroborated both results by the histological observations of samples of gastrocnemius muscle. These findings showed that this hemorrhagic metalloproteinase, possesses high edematogenic and myotoxic activities and, in despite of exhibiting a weak proteolytic activity, it is able to degrade fibrinogen. So, this enzyme would contribute markedly to the phatophysiology of the bothropic envenomation.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Pergamon-Elsevier Science Ltd
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
Hemorrhagin
dc.subject
Metalloproteinase
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Snake Venom
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Bothrops Alternatus
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Zoología, Ornitología, Entomología, Etología
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-05-09T14:20:03Z
dc.journal.volume
46
dc.journal.number
5
dc.journal.pagination
546-554
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Gay, Claudia Carolina. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Leiva, Laura Cristina Ana. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas y Naturales y Agrimensura; Argentina
dc.description.fil
Fil: Maruñak, Silvana. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina
dc.description.fil
Fil: Teibler, Gladys Pamela. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina
dc.description.fil
Fil: Acosta de Pérez, Ofelia. Universidad Nacional del Nordeste. Facultad de Ciencias Veterinarias; Argentina
dc.journal.title
Toxicon
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.toxicon.2005.06.019
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0041010105002308
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