SOME DIFFERENCES IN THE CONJUGATION OF O-AMINOPHENOL AND P-NITROPHENOL BY THE URIDINE DIPHOSPHATE TRANSGLUCURONYLASE OF MOUSE-LIVER HOMOGENATES.

1. Glucuronide synthesis from uridine diphosphate glucuronate and o-aminophenol or p-nitrophenol in the presence of uridine diphosphate transglucuronylase of mouse-liver homogenates has been studied with respect to inhibition by compounds known to be conjugated under the experimental conditions, and also by thiophenol. 2. Raising the o-aminophenol concentration decreased the inhibition of o-aminophenyl glucuronide synthesis by the alternative glucuronyl acceptors phenol, menthol and benzoic acid, but was without effect on that caused by p-nitrophenol and thiophenol. 3. Raising the p-nitrophenol concentration decreased or abolished the inhibition of p-nitrophenyl glucuronide synthesis due to phenol, menthol, benzoic acid, anthranilic acid, o-aminophenol and thiophenol. 4. The o-aminophenol system was much more readily inhibited by all compounds than the p-nitrophenol system. 5. In tris buffer, pH7.4, over 30% activation of the o-aminophenol system was achieved by 2mm-Mg(2+), but 10mm-Mg(2+) was inhibitory. The p-nitrophenol system showed only inhibition from 2mm-Mg(2+) upwards. 6. The results are discussed as suggesting that there are at least two uridine diphosphate transglucuronylases.