Abstract
The inhibitory potencies of different flavonoids for rat liver cytosolic glutathione S-transferase activity varied over 30-fold, depending on the pattern of hydroxylation, the presence of a C-2, C-3 double bond and the substitution of a hydroxyl group with a sugar moiety. Kinetic inactivation studies of the enzyme with the inhibitor quercetin revealed a non-competitive profile versus both glutathione and 1-chloro-2,4-dinitrobenzene.
MeSH terms
-
Animals
-
Cytosol / enzymology
-
Dinitrochlorobenzene / pharmacology
-
Flavonoids / administration & dosage
-
Flavonoids / chemistry
-
Flavonoids / pharmacology*
-
Glutathione / metabolism
-
Glutathione Transferase / antagonists & inhibitors*
-
Hydroxylation
-
Kinetics
-
Liver / enzymology*
-
Liver / ultrastructure
-
Male
-
Molecular Structure
-
Quercetin / pharmacology
-
Rats
-
Rats, Inbred Strains
-
Structure-Activity Relationship
Substances
-
Dinitrochlorobenzene
-
Flavonoids
-
Quercetin
-
Glutathione Transferase
-
Glutathione