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dc.contributor.authorHiguchi, D. A.
dc.contributor.authorBarbosa, C. M. V.
dc.contributor.authorBincoletto, C.
dc.contributor.authorChagas, J. R.
dc.contributor.authorMagalhaes, A.
dc.contributor.authorRichardson, M.
dc.contributor.authorSanchez, E. F.
dc.contributor.authorPesquero, J. B.
dc.contributor.authorAraujo, R. C.
dc.contributor.authorPesquero, J. L.
dc.date.accessioned2016-01-24T12:41:55Z
dc.date.available2016-01-24T12:41:55Z
dc.date.issued2007-03-01
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2006.10.010
dc.identifier.citationBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 89, n. 3, p. 319-328, 2007.
dc.identifier.issn0300-9084
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/29540
dc.description.abstractTwo proteins with phospholipase A(2) (PLA(2)) activity were purified to homogeneity from Bothrops leucurus (white-tailed-jararaca) snake venom through three chromatographic steps: Conventional gel filtration on Sephacryl S-200, ion-exchange on Q-Sepharose and reverse phase on Vydac C4 HPLC column. the molecular mass for both enzymes was estimated to be approximately 14 kDa by SDS-PAGE. the N-terminal sequences (48 residues) show that one enzyme presents lysine at position 48 and the other an aspartic acid in this position, and therefore they were designated blK-PLA(2) and blD-PLA(2) respectively. blK-PLA(2) presented negligible levels of PLA(2) activity as compared to that of blD-PLA(2). the PLA(2) activity of both enzymes is Ca2+-dependent. blD-PLA(2) did not have any effect upon platelet aggregation induced by arachidonic acid, ADP or collagen, but strongly inhibits coagulation and is able to stimulate Ehrlich tumor growth but not angiogenesis. (c) 2006 Elsevier Masson SAS. All rights reserved.en
dc.format.extent319-328
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.rightsAcesso restrito
dc.subjectBothrops leucurusen
dc.subjectPLA(2)en
dc.subjectplatelet aggregationen
dc.subjectblood coagulationen
dc.subjectangiogenesisen
dc.subjectsnake venomen
dc.titlePurification and partial characterization of two phospholipases A(2) from Bothrops leucurus (white-tailed-jararaca) snake venomen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniv Mogi Das Cruzes
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade Federal de Minas Gerais (UFMG)
dc.description.affiliationUniv Mogi Das Cruzes, BR-08780911 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.description.affiliationUniv Fed Minas Gerais, Dept Biophys, Belo Horizonte, MG, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, São Paulo, Brazil
dc.identifier.doi10.1016/j.biochi.2006.10.010
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000245998900006


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