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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/7558
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dc.contributor.authorStabeli, R. G.-
dc.contributor.authorMarcussi, S.-
dc.contributor.authorCarlos, G. B.-
dc.contributor.authorPietro, RCLR-
dc.contributor.authorSelistre-De-Araujo, H. S.-
dc.contributor.authorGiglio, JR-
dc.contributor.authorOliveira, E. B.-
dc.contributor.authorSoares, A. M.-
dc.date.accessioned2014-05-20T13:24:25Z-
dc.date.accessioned2016-10-25T16:45:07Z-
dc.date.available2014-05-20T13:24:25Z-
dc.date.available2016-10-25T16:45:07Z-
dc.date.issued2004-06-01-
dc.identifierhttp://dx.doi.org/10.1016/j.bmc.2004.03.049-
dc.identifier.citationBioorganic & Medicinal Chemistry. Oxford: Pergamon-Elsevier B.V., v. 12, n. 11, p. 2881-2886, 2004.-
dc.identifier.issn0968-0896-
dc.identifier.urihttp://hdl.handle.net/11449/7558-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/7558-
dc.description.abstractThe isolation and biochemical/enzymatic characterization of an L-amino acid oxidase, Balt-LAAO-I, from Bothrops alternates snake venom, is described. Balt-LAAO-I is an acidic glycoprotein, pI similar to 5.37, homodimeric, M-r similar to 123, 000, whose Nterminal sequence is ADVRNPLE EFRETDYEVL. It displays a high specificity toward hydrophobic and basic amino acids, while deglycosylation does not alter its enzymatic activity. Bait-LAAO-I induces platelet aggregation and shows bactericidal activity against Escherichia coli and Staphylococcus aureus. In addition, this enzyme is slightly hemorrhagic and induces edema in the mouse paw. Bait-LAAO-I is a multifunctional enzyme with promising relevant biotechnological and medical applications. (C) 2004 Elsevier Ltd. All rights reserved.en
dc.format.extent2881-2886-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectsnake venompt
dc.subjectL-amino acid oxidasept
dc.subjectBothrops alternatuspt
dc.subjectbactericidal effectpt
dc.subjectplatelet aggregationpt
dc.subjectbiotechnological applicationpt
dc.titlePlatelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venomen
dc.typeoutro-
dc.contributor.institutionUNAERP-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)-
dc.description.affiliationUNAERP, Ribeirao Preto, SP, Brazil-
dc.description.affiliationUNAERP, Dept Farm, Ribeirao Preto, SP, Brazil-
dc.description.affiliationUniv Estadual Paulista, UNESP, Fac Ciências Farmaceut, Dept Farm & Medicamentos, Araraquara, SP, Brazil-
dc.description.affiliationUniv Fed Sao Carlos, Dept Ciências Fisiol, BR-13560 Sao Carlos, SP, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, UNESP, Fac Ciências Farmaceut, Dept Farm & Medicamentos, Araraquara, SP, Brazil-
dc.identifier.doi10.1016/j.bmc.2004.03.049-
dc.identifier.wosWOS:000221676700008-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBioorganic & Medicinal Chemistry-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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