Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom

Página do item simplificado
dc.contributor.authorYonamine, Camila Miyagui [UNIFESP]
dc.contributor.authorKondo, Marcia Yuri [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorIcimoto, Marcelo Yudi [UNIFESP]
dc.contributor.authorBaptista, Gandhi R.
dc.contributor.authorYamane, Tetsuo
dc.contributor.authorOliveira, Vitor [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorLapa, Antonio José [UNIFESP]
dc.contributor.authorLima-Landman, Maria Teresa Riggio de [UNIFESP]
dc.contributor.authorHayashi, Mirian Akemi Furuie [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionInst Ciencias Mar UFC
dc.contributor.institutionUniv Estado Amazonas
dc.date.accessioned2016-01-24T14:28:02Z
dc.date.available2016-01-24T14:28:02Z
dc.date.issued2012-12-01
dc.description.abstractThis work describes for the first time the characterization of the enzymatic features of gyroxin, a serine protease from Crotalus durissus terrificus venom, capable to induce barrel rotation syndrome in rodents. Measuring the hydrolysis of the substrate ZFR-MCA, the optimal pH for proteolytic cleavage of gyroxin was found to be at pH 8.4. Increases in the hydrolytic activity were observed at temperatures from 25 degrees C to 45 degrees C, and increases of NaCl concentration up to 1 M led to activity decreases. the preference of gyroxin for Arg residues at the substrate P1 position was also demonstrated. Taken together, this work describes the characterization of substrate specificity of gyroxin, as well as the effects of salt and pH on its enzymatic activity. (C) 2012 Elsevier Masson SAS. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Farmacol, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationInst Ciencias Mar UFC, BR-60165081 Fortaleza, Ceara, Brazil
dc.description.affiliationUniv Estado Amazonas, Escola Super Ciencias Saude INCT, BR-69065001 Manaus, Amazonas, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Farmacol, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.format.extent2791-2793
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2012.07.020
dc.identifier.citationBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 94, n. 12, p. 2791-2793, 2012.
dc.identifier.doi10.1016/j.biochi.2012.07.020
dc.identifier.fileWOS000312517800039.pdf
dc.identifier.issn0300-9084
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/35517
dc.identifier.wosWOS:000312517800039
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectGyroxinen
dc.subjectCrotalusen
dc.subjectKineticen
dc.subjectEnzymaticen
dc.subjectSubstrateen
dc.subjectSpecificityen
dc.titleKinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venomen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Pacote Original
Agora exibindo 1 - 1 de 1
Imagem de Miniatura
Nome:
WOS000312517800039.pdf
Tamanho:
229.51 KB
Formato:
Adobe Portable Document Format
Descrição:
Baixar
Coleções
EPM - Artigos