Literature DB >> 6422795

Studies of UDP-glucuronosyltransferase activity toward eugenol, using a gas chromatographic method of measurement.

J A Boutin, G Siest, A M Batt, E Solheim, R R Scheline.   

Abstract

A method for the assay of uridine diphosphate (UDP)-glucuronosyltransferase activities toward some phenolic compounds and monoterpenoid alcohols is described. The method is based on the disappearance of the free substrate after incubation with microsomes and UDP-glucuronate. This disappearance is recorded using a gas chromatographic process. This method has been used, for example, to characterize the glucuronidation process of eugenol (4-allyl-2-methoxyphenol). The method could be extended to other substrates. Analytical conditions are given for some of them, especially monoterpenoid alcohols since the studies of their conjugations are a growing field of interest in evaluation of heterogeneity of UDP-glucuronosyltransferase. The method could also be used with other biological materials including cell suspension and crude liver biopsies.

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Year:  1983        PMID: 6422795     DOI: 10.1016/0003-2697(83)90752-2

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  1 in total

1.  Further validation of the Mulder and van Doorn kinetic procedure for the measurement of microsomal UDP-glucuronosyltransferase activities.

Authors:  B Antoine; J A Boutin; G Siest
Journal:  Biochem J       Date:  1988-06-15       Impact factor: 3.857

  1 in total

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