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. 1965 Apr;95(1):209–214. doi: 10.1042/bj0950209

Some differences in the conjugation of o-aminophenol and p-nitrophenol by the uridine diphosphate transglucuronylase of mouse-liver homogenates

I D E Storey 1
PMCID: PMC1215195  PMID: 14333559

Abstract

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-Mg2+, but 10mm-Mg2+ was inhibitory. The p-nitrophenol system showed only inhibition from 2mm-Mg2+ upwards. 6. The results are discussed as suggesting that there are at least two uridine diphosphate transglucuronylases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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