Kinetics of the reduction of oxaloacetate catalyzed by mitochondrial malate dehydrogenase of Toxocara canis muscle.
Comp Biochem Physiol B
; 98(2-3): 333-7, 1991.
Article
em En
| MEDLINE
| ID: mdl-1873988
1. The reaction of reduction of oxaloacetate to L-malate in the presence of NADH catalyzed by mitochondrial malate dehydrogenase (EC 1.1.1.37) of Toxocara canis muscle has been studied. 2. The data obtained in initial velocity experiments as well as those involving product inhibition suggest that the reaction mechanism is of the sequential type with a kinetically significant ternary complex and in which the coenzymes bind to the free enzyme. 3. The kinetic parameters, including the inhibition constant for NADH were estimated by non-linear regression analysis using the appropriate rate equations.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxaloacetatos
/
Toxocara
/
Malato Desidrogenase
/
Mitocôndrias Musculares
Limite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Reino Unido