Absolute quantification of human uridine-diphosphate glucuronosyl transferase (UGT) enzyme isoforms 1A1 and 1A6 by tandem LC-MS.

@article{Fallon2008AbsoluteQO,
  title={Absolute quantification of human uridine-diphosphate glucuronosyl transferase (UGT) enzyme isoforms 1A1 and 1A6 by tandem LC-MS.},
  author={John K Fallon and David E Harbourt and Saber H Maleki and Fay K Kessler and Joseph K. Ritter and Philip D. Coleridge Smith},
  journal={Drug metabolism letters},
  year={2008},
  volume={2 3},
  pages={210-22}
}
UGT enzymes catalyze the formation of glucuronic acid conjugates. Specifically selected representative stable isotope (C(13), N(15)) labeled peptide internal standards of each enzyme were employed to quantify UGTs 1A1 and 1A6 by LC-MS/MS using isotope dilution techniques. Inter day variability (n=5) for human liver microsomes was <or= 8.0 % for UGT1A1 and <or= 19 % for UGT1A6. Comparison within a human liver microsomal library showed a strong correlation with Western blot for UGT1A1… CONTINUE READING
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