dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorStabeli, R. G.
dc.creatorMarcussi, S.
dc.creatorCarlos, G. B.
dc.creatorPietro, RCLR
dc.creatorSelistre-De-Araujo, H. S.
dc.creatorGiglio, JR
dc.creatorOliveira, E. B.
dc.creatorSoares, A. M.
dc.date2014-05-20T13:24:25Z
dc.date2016-10-25T16:45:07Z
dc.date2014-05-20T13:24:25Z
dc.date2016-10-25T16:45:07Z
dc.date2004-06-01
dc.date.accessioned2017-04-05T20:00:01Z
dc.date.available2017-04-05T20:00:01Z
dc.identifierBioorganic & Medicinal Chemistry. Oxford: Pergamon-Elsevier B.V., v. 12, n. 11, p. 2881-2886, 2004.
dc.identifier0968-0896
dc.identifierhttp://hdl.handle.net/11449/7558
dc.identifierhttp://acervodigital.unesp.br/handle/11449/7558
dc.identifier10.1016/j.bmc.2004.03.049
dc.identifierWOS:000221676700008
dc.identifierhttp://dx.doi.org/10.1016/j.bmc.2004.03.049
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/856169
dc.descriptionThe 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.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBioorganic & Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectsnake venom
dc.subjectL-amino acid oxidase
dc.subjectBothrops alternatus
dc.subjectbactericidal effect
dc.subjectplatelet aggregation
dc.subjectbiotechnological application
dc.titlePlatelet aggregation and antibacterial effects of an L-amino acid oxidase purified from Bothrops alternatus snake venom
dc.typeOtro


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