Comparison of hydrolytic and conjugative biotransformation pathways in horse, cattle, pig, broiler chick, rabbit and rat liver subcellullar fractions.
To complete a studyaimed at investigating the pattern of the basal activities of liver xenobioticmetabolizing enzymes in major and minor species intended for meat production, microsomal carboxylesterases and some conjugating enzyme activities were determined and compared in liver preparations from horses, cattle, pigs, rabbits and broiler chicks, using the rat as a reference species. Horses and broiler chicks exhibited a lower microsomal carboxylesterase activity towards indophenyl or p-nitrophenyl acetate than that measured in cattle or pig subfractions. Among food-producing species, the rate of glucuronidation of either 1-naphthol or p-nitrophenol was in the order pigs approximately rabbits > horses >> cattle > broiler chicks. The widest variations were observed in the acetylation capacity towards p-aminobenzoic acid or isoniazid, which in rabbits was 3-fold to 11-fold greater than that displayed by any other examined species; low but measurable activities were found in equine and bovine cytosols. The activity of cytosolic glutathione S-transferase (GST) accepting the general substrate 1-chloro-2,4-dinitrobenzene was significantly higher in rabbits, horses and pigs than in rat, broiler chicks and cattle. Finally, an uneven pattern of activity towards the other tested GST substrates - 3,4-dichloronitrobenzene, ethacrinic acid or 1,2-epoxybutane - was observed, possibly reflecting the species-related expression of different GST classes; in this respect, the conjugative capacity displayed by horses was higher than or comparable to that found in the other food-producing species.
Gusson
F
F
Department of Animal Pathology, Division of Pharmacology and Toxicology, University of Turin, Via Leonardo da Vinci 44, I-10095, Grugliasco.
Carletti
M
M
Albo
A Giuliano
AG
Dacasto
M
M
Nebbia
C
C
D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D001711:Biotransformation / Q000502:physiology*; D008099:Liver / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D013045:Species Specificity; D013379:Substrate Specificity; D015262:Xenobiotics / Q000378:metabolism
D015262:Xenobiotics; D000123:Acetyltransferases