Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Más filtros











Base de datos
Idioma
Intervalo de año de publicación
2.
Zh Evol Biokhim Fiziol ; 12(3): 227-32, 1976.
Artículo en Ruso | MEDLINE | ID: mdl-1085084

RESUMEN

The resistances to heat and trypsin hydrolysis served as indirect indices of conformational flexibility of glutamate dehydrogenase molecules. No difference in heat resistance was found between crystalline eletrophoretically homogeneous preparations of glutamate dehydrogenase from liver mitochondria of two species of frogs, the more southern Rana ridibunda and the more northern R. temporaria. However, glutamate dehydrogenase from R. ridibunda is digested by trypsin at a lower rate than that from R. temporaria, which may be explained by its lower conformational flexibility. Therefore positive correlation between conformational flexibility of glutamate dehydrogenase and mean ambient temperature of the species studied is revealed only with respect to resistance to proteolysis.


Asunto(s)
Glutamato Deshidrogenasa/metabolismo , Mitocondrias Hepáticas/enzimología , Animales , Calor , Rana temporaria/metabolismo , Ranidae , Especificidad de la Especie , Tripsina/metabolismo
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA