Heterogeneity of hepatic UDP-glucuronosyltransferase activities: investigations of isoenzymes involved in p-nitrophenol glucuronidation.

1. UDP-Glucuronosyltransferase (UGT, EC 2.1.4.17) has been measured routinely with para-nitrophenol (pNP) because the UGT assay using this substrate is easy to assess and run. 2. This compound has been used in several studies as a substrate for purification of the enzyme. 3. In the present work, we characterize the para-nitrophenol-conjugating activity. 4. An analysis of kinetics of para-nitrophenol conjugation obtained from various biological sources (various tissues and various species) leads us to the conclusion that at least three isoenzymes are responsible for this activity in the rat. 5. Both UGT-(testosterone) and the 3-methylcholanthrene-inducible form previously described in the literature, may be responsible for the activity, whilst a highly specific form (UGT-phenol) is reported here for the first time. 6. This work is intended to lay down the basis of further investigations, including purification of the highly specific isoform.