Isolation of a new L-amino acid oxidase from Crotalus durissus cascavella venom

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dc.contributor.authorToyama, M. H.
dc.contributor.authorToyama, D. D.
dc.contributor.authorPassero, LFD
dc.contributor.authorLaurenti, M. D.
dc.contributor.authorCorbett, C. E.
dc.contributor.authorTomokane, T. Y.
dc.contributor.authorFonseca, F. V.
dc.contributor.authorAntunes, E.
dc.contributor.authorJoazeiro, P. P.
dc.contributor.authorBeriam, LOS
dc.contributor.authorMartins, MAC
dc.contributor.authorMonteiro, HSA
dc.contributor.authorFonteles, M. C.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Mackenzie
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionInst Biol Campinas
dc.contributor.institutionUFC
dc.date.accessioned2014-05-20T15:25:50Z
dc.date.available2014-05-20T15:25:50Z
dc.date.issued2006-01-01
dc.description.abstractA novel L-amino acid oxidase (LAO) (Casca LAO) from Crotalus durissus cascavella venom was purified to a high degree of molecular homogeneity using a combination of molecular exclusion and ion-exchange chromatography system. The purified monomer of LAO presented a molecular mass of 68 kDa and pI estimated in 5.43, which were determined by two-dimensional electrophoresis. The 71st N-terminal amino acid sequence of the LAO from Crotalus durissus cascavella presented a high amino acid sequence similarities with other LAOs from Colloselasma rhosostoma, Crotalus adamanteus, Agkistrodon h. blomhoffi, Agkistrodon h. halys and Trimeresurus stejnegeri. LAO displayed a Michaelis-Menten behavior with a kilometer of 46.7 mu M and an optimum pH for enzymatic activity of 6.5. Casca LAO induced a dose-dependent platelet aggregation, which was abolished by catalase and inhibited by indomethacin and aspirin. These results suggest that the production of H2O2 is involved in subsequent activation of inflammatory enzymes, such as thromboxane. Casca LAO also inhibited the bacterial Growth of Gram-negative (Xanthomonas axonopodis pv passiflorae) and Gram-positive (S. mutans) strains. Electron microscopy assessments of both bacterial strains suggest that the hydrogen peroxide produced by LAO induce bacterial membrane rupture and consequently loss of cytoplasmatic content. This LAO exhibited a high antileishmanic activity against the promastigote of Leishmania amazonensis in vitro, its activity was dependent on the production of hydrogen peroxide, and the 50% inhibitory concentration was estimated in 2.39 mu g/ml. (C) 2005 Elsevier Ltd. All rights reserved.en
dc.description.affiliationUNESP, São Paulo, Brazil
dc.description.affiliationUniv Mackenzie, Fac Ciências Biol Exatas & Expt, São Paulo, Brazil
dc.description.affiliationUSP, Lab Patol Molestias Infecc, Dept Patol, Fac Med, BR-09500900 São Paulo, Brazil
dc.description.affiliationUniv Estadual Campinas, Dept Farmacol, Fac Ciências Med, São Paulo, Brazil
dc.description.affiliationUniv Estadual Campinas, Dept Histol, Inst Biol, São Paulo, Brazil
dc.description.affiliationInst Biol Campinas, Lab Bacteriol Vegetal, Ctr Expt, São Paulo, Brazil
dc.description.affiliationUFC, Fac Med, Fortaleza, Ceara, Brazil
dc.description.affiliationUnespUNESP, São Paulo, Brazil
dc.format.extent47-57
dc.identifierhttp://dx.doi.org/10.1016/j.toxicon.2005.09.008
dc.identifier.citationToxicon. Oxford: Pergamon-Elsevier B.V., v. 47, n. 1, p. 47-57, 2006.
dc.identifier.doi10.1016/j.toxicon.2005.09.008
dc.identifier.issn0041-0101
dc.identifier.urihttp://hdl.handle.net/11449/36176
dc.identifier.wosWOS:000235381200006
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofToxicon
dc.relation.ispartofjcr2.352
dc.relation.ispartofsjr0,692
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectCrotalus durissus cascavellapt
dc.subjectantibacterialpt
dc.subjectantimicrobialpt
dc.subjecthydrogen peroxidept
dc.subjectgyroxinpt
dc.subjectleishmanicidalpt
dc.titleIsolation of a new L-amino acid oxidase from Crotalus durissus cascavella venomen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.orcid0000-0003-2201-8247[8]
unesp.author.orcid0000-0001-6836-3084[2]
unesp.author.orcid0000-0002-1431-6829[6]
unesp.author.orcid0000-0002-5986-6381[3]

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