通过串联液相色谱-质谱联用技术对人尿苷二磷酸葡萄糖醛酸基转移酶（UGT）同工酶1A1和1A6进行绝对定量分析。
Absolute quantification of human uridine-diphosphate glucuronosyl transferase (UGT) enzyme isoforms 1A1 and 1A6 by tandem LC-MS.
作者信息
Fallon John K, Harbourt David E, Maleki Saber H, Kessler Fay K, Ritter Joseph K, Smith Philip C
机构信息
Division of Molecular Pharmaceutics, School of Pharmacy, University of North Carolina at Chapel Hill, NC 27599, USA.
出版信息
Drug Metab Lett. 2008 Aug;2(3):210-22. doi: 10.2174/187231208785425764.
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 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.
UGT酶催化葡糖醛酸缀合物的形成。通过使用同位素稀释技术的液相色谱-串联质谱法（LC-MS/MS），采用每种酶的特定选择的代表性稳定同位素（C(13)、N(15)）标记的肽内标来定量UGT1A1和UGT1A6。人肝微粒体的日间变异性（n = 5），UGT1A1为≤8.0%，UGT1A6为≤19%。在人肝微粒体文库中的比较显示，UGT1A1浓度与蛋白质印迹法有很强的相关性（r = 0.988）。所呈现的数据表明，使用蛋白质内特征肽的LC-MS/MS分析可以建立一种准确且可重复的UGT绝对定量方法。
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