Oxidation of acetylacetone catalyzed by horseradish peroxidase in the absence of hydrogen peroxide

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dc.contributor.authorRodrigues, Ana Paula
dc.contributor.authorda Fonseca, Luiz Marcos
dc.contributor.authorde Faria Oliveira, Olga M.
dc.contributor.authorBrunetti, Iguatemy Lourenço [UNESP]
dc.contributor.authorXimenes, Valdecir Farias [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:24:26Z
dc.date.available2014-05-20T13:24:26Z
dc.date.issued2006-12-01
dc.description.abstractHorseradish peroxidase (HRP) is a plant enzyme widely used in biotechnology, including antibody-directed enzyme prodrug therapy (ADEPT). Here, we showed that HRP is able to catalyze the autoxidation of acetylacetone in the absence of hydrogen peroxide. This autoxidation led to generation of methylglyoxal and reactive oxygen species. The production of superoxide anion was evidenced by the effect of superoxide dismutase and by the generation of oxyperoxidase during the enzyme turnover. The HRP has a high specificity for acetylacetone, since the similar beta-dicarbonyls dimedon and acetoacetate were not oxidized. As this enzyme prodrug combination was highly cytotoxic for neutrophils and only requires the presence of a non-human peroxidase and acetylacetone, it might immediately be applied to research on the ADEPT techniques. The acetylacetone could be a starting point for the design of new drugs applied in HRP-related ADEPT techniques. (c) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP, Fac Ciências Farmaceut Araraquara, Dept Anal Clin, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUNESP, Inst Quim, Dept Biotecnol, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Fac Ciências, Dept Quim, Bauru, SP, Brazil
dc.description.affiliationUnespUNESP, Fac Ciências Farmaceut Araraquara, Dept Anal Clin, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP, Inst Quim, Dept Biotecnol, BR-14801902 Araraquara, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciências, Dept Quim, Bauru, SP, Brazil
dc.format.extent1755-1761
dc.identifierhttp://dx.doi.org/10.1016/j.bbagen.2006.09.008
dc.identifier.citationBiochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1760, n. 12, p. 1755-1761, 2006.
dc.identifier.doi10.1016/j.bbagen.2006.09.008
dc.identifier.issn0304-4165
dc.identifier.lattes4066413997908572
dc.identifier.urihttp://hdl.handle.net/11449/7572
dc.identifier.wosWOS:000242459500001
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimica et Biophysica Acta: General Subjects
dc.relation.ispartofjcr3.679
dc.relation.ispartofsjr1,671
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjecthorseradish peroxidasept
dc.subjectacetylacetonept
dc.subjectmethylglyoxalpt
dc.subjectreactive oxygen speciespt
dc.subjectantibody-directed enzyme prodrug therapypt
dc.titleOxidation of acetylacetone catalyzed by horseradish peroxidase in the absence of hydrogen peroxideen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes4066413997908572
unesp.author.orcid0000-0003-2636-3080[5]
unesp.author.orcid0000-0003-4927-7599[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências, Baurupt
unesp.departmentQuímica - FCpt

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Artigos - Análises Clínicas - FCFAR
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