Lactate dehydrogenase from cultured Aedes albopictus cells: kinetic and isozyme analysis
An. acad. bras. ciênc
;
59(4): 433-7, 1987. tab
Artículo
en Inglés
| LILACS
| ID: lil-94855
RESUMO
L (+) lactate dehydrogenase (LDH) activity from cultured cells of Aedes albopictus was studies as a kinetic model of carbohydrate metabolism. Enzyme kinetics were studied in the forward (lactate as substrte) and reverse (pyruvate as substrate) reactions and the apparent Km values were obtained showing LDH higher affinity for pyruvate. The Hill coefficient values for each substrate were similar and indicate the existence of only one binding site on the enzyme. Isozyme analysis on cellulose-acetate electrophoresis presented a singe band of LDH which preumably is of the LDH-5 type. The results obtained contribute to the assumption that Aedes albopictus cells have a predominance of anaerobic metabolism
Buscar en Google
Índice:
LILACS (Américas)
Asunto principal:
Aedes
/
L-Lactato Deshidrogenasa
Límite:
Animales
Idioma:
Inglés
Revista:
An. acad. bras. ciênc
Asunto de la revista:
Ciencia
Año:
1987
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS