Purification and renal effects of phospholipase A(2) isolated from Bothrops insularis venom

Página do item simplificado
dc.contributor.authorMachado Braga, Marcus Davis
dc.contributor.authorCosta Martins, Alice Maria
dc.contributor.authorAlves, Claudnio Diogenes
dc.contributor.authorde Menezes, Dalgimar Beserra
dc.contributor.authorMartins, Rene Duarte
dc.contributor.authorFerreira Barbosa, Paulo Sergio
dc.contributor.authorde Sousa Oliveira, Isadora Maria
dc.contributor.authorToyama, Marcos Hikarl [UNESP]
dc.contributor.authorToyama, Daniela Oliveira
dc.contributor.authordos Santos Diz Filho, Eduardo Brito [UNESP]
dc.contributor.authorRamos Fagundes, Fabio Henrique [UNESP]
dc.contributor.authorFonteles, Manasses Claudino
dc.contributor.authorAzul Monteiro, Helena Serra
dc.contributor.institutionUniversidade Federal do Ceará (UFC)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionPresbiterian Mackenz Univ
dc.date.accessioned2014-05-20T13:12:20Z
dc.date.available2014-05-20T13:12:20Z
dc.date.issued2008-02-01
dc.description.abstractBothrops insularis venom contains a variety of substances presumably responsible for several pharmacological effects. We investigated the biochemical and biological effects of phospholipase A(2) protein isolated from B. insularis venom and the chromatographic profile showed 7 main fractions and the main phospholipase A(2) (PLA(2)) enzymatic activity was detected in fractions IV and V. Fraction IV was submitted to a new chromatographic procedure on ion exchange chromatography, which allowed the elution of 5 main fractions designated as lV-1 to IV-5, from which lV-4 constituted the main fraction. The molecular homogeneity of this fraction was characterized by high-performance liquid chromatography (HPLC) and demonstrated by mass spectrometry (MS), which showed a molecular mass of 13984.20 Da; its N-terminal sequence presented a high amino acid identity (up to 95%) with the PLA(2) of Bothrops jararaca and Bothrops asper. Phospholipase A(2) isolated from B. insularis (Bi PLA(2)) venom (10 mu g/mL) was also studied as to its effect on the renal function of isolated perfused kidneys of Wistar rats (n = 6). Bi PLA(2) increased perfusion pressure (PP), renal vascular resistance (RVR), urinary flow (UF) and glomerular filtration rate (GFR). Sodium (%TNa+) and chloride tubular reabsorption (%TCl-) decreased at 120 min, without alteration in potassium transport. In conclusion, PLA(2) isolated from B. insularis venom promoted renal alterations in the isolated perfused rat kidney. (c) 2007 Elsevier Ltd. All rights reserved.en
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Fisiol & Farmacol, Fac Med, Unidad Pesquisas Clin UFC, BR-60420970 Fortaleza, Ceara, Brazil
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Pathol, BR-60420970 Fortaleza, Ceara, Brazil
dc.description.affiliationUniversidade Federal do Ceará (UFC), Dept Clin & Toxicol Analyses, BR-60420970 Fortaleza, Ceara, Brazil
dc.description.affiliationPaulista State Univ UNESP, Sao Vicente Unity, São Paulo, Brazil
dc.description.affiliationPresbiterian Mackenz Univ, Biol Sci Exact & Expt Fac, São Paulo, Brazil
dc.description.affiliationUnespPaulista State Univ UNESP, Sao Vicente Unity, São Paulo, Brazil
dc.format.extent181-190
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2007.08.017
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V. Ltd, v. 51, n. 2, p. 181-190, 2008.
dc.identifier.doi10.1016/j.toxicon.2007.08.017
dc.identifier.issn0041-0101
dc.identifier.lattes8573195327542061
dc.identifier.urihttp://hdl.handle.net/11449/315
dc.identifier.wosWOS:000253389900003
dc.language.isoeng
dc.publisherPergamon-Elsevier B.V. Ltd
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectBothrops insularisen
dc.subjectphospholipase A(2)en
dc.subjectrenal biological activityen
dc.titlePurification and renal effects of phospholipase A(2) isolated from Bothrops insularis venomen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderPergamon-Elsevier B.V. Ltd
unesp.advisor.lattes8573195327542061
unesp.author.orcid0000-0001-6836-3084[9]
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências, São Vicentept

Arquivos

Licença do Pacote
Agora exibindo 1 - 2 de 2
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:

Coleções

Artigos - Ciências Biológicas - São Vicente