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
Article
Dans Anglais
| 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.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
langue:
Anglais
Texte intégral:
J Biosci
Année:
1987
Type:
Article
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