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

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

Author Yonamine, Camila Miyagui Autor UNIFESP Google Scholar
Kondo, Marcia Yuri Autor UNIFESP Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Icimoto, Marcelo Yudi Autor UNIFESP Google Scholar
Baptista, Gandhi R. Google Scholar
Yamane, Tetsuo Google Scholar
Oliveira, Vitor Autor UNIFESP Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Lapa, Antonio José Autor UNIFESP Google Scholar
Lima-Landman, Maria Teresa Riggio de Autor UNIFESP Google Scholar
Hayashi, Mirian Akemi Furuie Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Inst Ciencias Mar UFC
Univ Estado Amazonas
Abstract This 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.
Keywords Gyroxin
Crotalus
Kinetic
Enzymatic
Substrate
Specificity
Language English
Sponsor Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Date 2012-12-01
Published in Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 94, n. 12, p. 2791-2793, 2012.
ISSN 0300-9084 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 2791-2793
Origin http://dx.doi.org/10.1016/j.biochi.2012.07.020
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000312517800039
URI http://repositorio.unifesp.br/handle/11600/35517

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