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Drug Metabolism Letters

Editor-in-Chief

ISSN (Print): 1872-3128
ISSN (Online): 1874-0758

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

Author(s): John K. Fallon, David E. Harbourt, Saber H. Maleki, Fay K. Kessler, Joseph K. Ritter and Philip C. Smith

Volume 2, Issue 3, 2008

Page: [210 - 222] Pages: 13

DOI: 10.2174/187231208785425764

Price: $65

Abstract

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.

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


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