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Absolute Quantification of Human Uridine-Diphosphate Glucuronosyl Transferase (UGT) Enzyme Isoforms 1A1 and 1A6 By Tandem LC-MS

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UGT enzymes catalyze the formation of glucuronic acid conjugates. Specifically selected representative stable isotope (C13, N15) 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 ≤ 8.0 % for UGT1A1 and ≤ 19 % for UGT1A6. Comparison within a human liver microsomal library showed a strong correlation with Western blot for UGT1A1 concentrations (r=0.988). The data presented indicates that an accurate and reproducible method for UGT absolute quantification can be established using LC-MS/MS analysis of characteristic peptides within the protein.





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Keywords: LC-MS/MS; UGT; absolute quantification; quantitative proteomics; stable isotope labeled synthetic peptides; triple quadrupole

Document Type: Research Article

Publication date: August 1, 2008

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  • Drug Metabolism Letters publishes short papers on major advances in all areas of drug metabolism and disposition. The emphasis will be on publishing quality papers very rapidly. Letters will be processed rapidly by taking full advantage of the Internet technology for both the submission and review of manuscripts. The journal covers the following areas:

    In vitro systems including CYP-450; enzyme induction and inhibition; drug-drug interactions and enzyme kinetics; pharmacokinetics, toxicokinetics, species scaling and extrapolations; P-glycoprotein and transport carriers; target organ toxicity and interindividual variability; drug metabolism and disposition studies; extrahepatic metabolism; phase I and phase II metabolism; recent developments for the identification of drug metabolites, reactive intermediate and glutathione conjugates.
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