4-nitrocatechol and 7-hydroxycoumarin

Glucuronidation and sulfation of 1-naphthol, 7-hydroxycoumarin, 4-nitrocatechol and phenolphthalein were studied in rabbit lung and liver. Pulmonary UDP-glucuronyltransferase and sulfotransferase activities in subcellular fractions were approximately 20-50% of those determined in the liver. Ethanol did not markedly induce these enzymes in either tissue. Glucuronidation and sulfation of 1-naphthol and 7-hydroxycoumarin were also studied in the isolated perfused rabbit lung as an intact cell model. Neither glucuronidation nor sulfation of 1-naphthol was observed. The absence of conjugate formation was due neither to the presence of beta-glucuronidase and/or sulfatase, nor to alternative biotransformation pathways. About 35% of the initial 7-hydroxycoumarin was conjugated, the majority being sulfate conjugate (14.4 nmol/h) with only minor amounts (0.12%) of the glucuronide. These results indicate the importance of studying both whole organ and in vitro metabolism.

Topics: Animals; Catechols; Chromatography, Thin Layer; Ethanol; Glucuronates; Glucuronosyltransferase; In Vitro Techniques; Liver; Lung; Male; Methylcholanthrene; Naphthols; Phenobarbital; Phenolphthalein; Phenolphthaleins; Rabbits; Subcellular Fractions; Sulfates; Sulfotransferases; Umbelliferones