Enzymes of carbohydrate metabolism of Cotugnia digonopora and their activity in the presence of anthelmintics, in vitro.
J Biosci
;
1987 Sept; 12(3): 239-247
Artículo
en Inglés
| IMSEAR
| ID: sea-160584
ABSTRACT
Cotugnia digonopora, a fowl cycllophyllidean cestode, was found to possess most of the enzymes, associated with the glycolytic sequence and phosphoenolpyruvate branch point, in the cytosol fraction. Enzymes of malate metabolism were predominantly mitrochondrial. Anthelmintic agents inhibited hexokinase, phosphofructokinase, glucose-6- phosphate dehydrogenase, malate dehydrogenase, fumarate reductase, and malic enzyme. In intact worms this effect was significantly reduced. However, the activities of glycogen Phosphorylase and pyruvate kinase were significantly enhanced.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Idioma:
Inglés
Revista:
J Biosci
Año:
1987
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS