Inhibition of mitochondrial oxidative phosphorylation and its electron transport pathway by a polycation in vitro.
Indian J Biochem Biophys
;
1993 Feb; 30(1): 49-53
Article
Dans Anglais
| IMSEAR
| ID: sea-28941
ABSTRACT
Effect of the polycation on oxidative phosphorylation in the rat liver mitochondria has been studied. Both oxygen uptake and coupled phosphorylation were progressively inhibited by increasing concentration of the polycation, as observed with NAD-linked substrates, succinate and ascorbate+TMPD which activates the terminal part of the respiratory chain. NADH oxidase, NADH dehydrogenase and cytochrome oxidase were strongly inhibited by the polycation, 80-90% of the activity being lost at an inhibitor concentration of 100 microM. Succinate oxidase and succinate dehydrogenase were inhibited 60-66% at 100 microM concentration of the polycation. The polycation inhibited the uncoupler 2,4-dinitrophenol stimulated ATPase activity both in presence and absence of Mg2+ ions. The polycation also inhibited salt-induced volume change.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Phosphorylation oxydative
/
Polyamines
/
Polymères
/
Rats
/
Mâle
/
Mitochondries du foie
/
Transport d'électrons
/
Animaux
/
NAD
langue:
Anglais
Texte intégral:
Indian J Biochem Biophys
Année:
1993
Type:
Article
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