dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.contributorInst Ciencias Mar UFC
dc.contributorUniv Estado Amazonas
dc.creatorYonamine, Camila Miyagui [UNIFESP]
dc.creatorKondo, Marcia Yuri [UNIFESP]
dc.creatorJuliano, Maria Aparecida [UNIFESP]
dc.creatorIcimoto, Marcelo Yudi [UNIFESP]
dc.creatorBaptista, Gandhi R.
dc.creatorYamane, Tetsuo
dc.creatorOliveira, Vitor [UNIFESP]
dc.creatorJuliano, Luiz [UNIFESP]
dc.creatorLapa, Antonio José [UNIFESP]
dc.creatorLima-Landman, Maria Teresa Riggio de [UNIFESP]
dc.creatorHayashi, Mirian Akemi Furuie [UNIFESP]
dc.date.accessioned2016-01-24T14:28:02Z
dc.date.accessioned2023-09-04T19:19:33Z
dc.date.available2016-01-24T14:28:02Z
dc.date.available2023-09-04T19:19:33Z
dc.date.created2016-01-24T14:28:02Z
dc.date.issued2012-12-01
dc.identifierBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 94, n. 12, p. 2791-2793, 2012.
dc.identifier0300-9084
dc.identifierhttp://repositorio.unifesp.br/handle/11600/35517
dc.identifierWOS000312517800039.pdf
dc.identifier10.1016/j.biochi.2012.07.020
dc.identifierWOS:000312517800039
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8625223
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.
dc.languageeng
dc.publisherElsevier B.V.
dc.relationBiochimie
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.rightsAcesso aberto
dc.subjectGyroxin
dc.subjectCrotalus
dc.subjectKinetic
dc.subjectEnzymatic
dc.subjectSubstrate
dc.subjectSpecificity
dc.titleKinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom
dc.typeArtigo


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