Hydrophilic interaction liquid chromatography (HILIC) in proteomics

被引：211
|
作者：
Boersema, Paul J. [1 ,2 ]
Mohammed, Shabaz [1 ,2 ]
Heck, Albert J. R. [1 ,2 ]
机构：
[1] Bijvoet Ctr Biomol Res, Biomol Mass Spectrometry & Proteom Grp, NL-3584 CA Utrecht, Netherlands
[2] Univ Utrecht, Utrecht Inst Pharmaceut Sci, NL-3584 CA Utrecht, Netherlands
来源：
ANALYTICAL AND BIOANALYTICAL CHEMISTRY | 2008年 / 391卷 / 01期
关键词：
HILIC; proteomics; post-translational modification; two-dimensional liquid chromatography;
D O I：
10.1007/s00216-008-1865-7
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
In proteomics, nanoflow multidimensional chromatography is now the gold standard for the separation of complex mixtures of peptides as generated by in-solution digestion of whole-cell lysates. Ideally, the different stationary phases used in multidimensional chromatography should provide orthogonal separation characteristics. For this reason, the combination of strong cation exchange chromatography (SCX) and reversed-phase (RP) chromatography is the most widely used combination for the separation of peptides. Here, we review the potential of hydrophilic interaction liquid chromatography (HILIC) as a separation tool in the multidimensional separation of peptides in proteomics applications. Recent work has revealed that HILIC may provide an excellent alternative to SCX, possessing several advantages in the area of separation power and targeted analysis of protein post-translational modifications.
引用
收藏
页码：151 / 159
页数：9
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