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Separation by FPLC chromatofocusing of UDP‐glucosyltransferases from three developmental stages of Drosophila melanogaster
Author(s) -
Rausell Carolina,
Llorca Julia,
Real M. Dolores
Publication year - 1997
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1997)34:3<347::aid-arch8>3.0.co;2-r
Subject(s) - chromatofocusing , fast protein liquid chromatography , xanthurenic acid , biology , biochemistry , glucosyltransferase , isozyme , melanogaster , glucosyltransferases , drosophila melanogaster , chromatography , enzyme , isoelectric point , chemistry , amino acid , tryptophan , gene
Variation of UDP‐glucosyltransferase activity, during Drosophila melanogaster development, was analyzed. The endogenous metabolite xanthurenic acid and the xenobiotic compounds 1‐naphthol and 2‐naphthol were used as substrates. Developmentally regulated differences were observed for the three substrates, suggesting the presence of UDP‐glucosyltransferase isoenzymes. This was further confirmed by FPLC chromatofocusing on a Mono P column: seven peaks of UDP‐glucosyltransferase activity (pHs: ≥6.3, 5.8, 5.5, 4.9, 4.5, 4.2, ≤4.0) with either single or overlapping substrate specificity were detected. A single xanthurenic acid:UDP‐glucosyltransferase activity (pl 5.8) was found throughout development. In contrast, a gradual increase in the number of 2‐napthol:UDP‐glucosyltransferase isoenzymes (pl from 6.3 to 4.0) was observed during development, whereas no isoenzymes specific for 1‐naphthol were resolved. Based on the distribution and substrate specificity of the eluted peaks in the three developmental stages analyzed, the presence of seven or possibly eight UDP‐glucosyltransferase isoenzymes is proposed. Arch. Insect Biochem. Physiol. 34:347–358, 1997. © 1997 Wiley‐Liss, Inc.