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. 1971 Dec;125(4):991–997. doi: 10.1042/bj1250991

Properties of Lubrol-extracted uridine diphosphate glucuronyltransferase

R D Howland 1,*, A Burkhalter 1, A J Trevor 1, S Hegeman 1, D Y Shirachi 1
PMCID: PMC1178261  PMID: 5144269

Abstract

1. A partially purified UDP-glucuronyltransferase was obtained by extracting rat liver microsomal preparations with Lubrol, a non-ionic detergent. 2. The soluble enzyme catalysed conjugation of both o-aminophenol and p-nitrophenol and was extremely stable when compared with untreated microsomal preparations. 3. The characteristics of the conjugation of the two phenols were found to differ with respect to pH optimum, bivalent cation requirement and Michaelis constants, suggesting that more than one enzyme is involved in the conjugation reaction.

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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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