Affiliation:
1. Departamento de Química-Física, E. U. Politécnia de Albacete, Universidad de Castilla-La Mancha, Albacete, spain.
2. Departamento de Bioquímica y Biología Molecular, Facultad de Biología, Universidad de Murcia, E-30100 Espinardo, Murcia, Spain
Abstract
The Michaelis constant of tyrosinase for oxygen in the presence of monophenols and o-diphenols, which generate a cyclizable o-quinone, has been studied. This constant depends on the nature of the monophenol and o-diphenol and is always lower in the presence of the former than of the latter. From the mechanism proposed for tyrosinase and from its kinetic analysis [Rodríguez-López, J. N., Tudela, J., Varón, R., García-Carmona, F. and García-Cánovas, F. (1992) J. Biol. Chem. 267, 3801-3810] a quantitative ratio has been established between the Michaelis constants for oxygen in the presence of monophenols and their o-diphenols. This ratio is used for the determination of the Michaelis constant for oxygen with monophenols when its value cannot be calculated experimentally.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
60 articles.
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