Application of electrostatic repulsion hydrophilic interaction chromatography to the characterization of proteome, glycoproteome, and phosphoproteome using nano LC-MS/MS

Piliang Hao, Huoming Zhang, Siu Kwan Sze*

*Corresponding author for this work

    Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

    6 Scopus citations

    Abstract

    In shotgun proteomics, peptide fractionation is essential for in-depth characterization of proteomes and the mapping of protein posttranslational modifications. Recently, a mix-mode chromatography [i.e., electrostatic repulsion hydrophilic interaction chromatography (ERLIC)] has been developed and found to be a versatile method in proteome characterization. Here, we use ERLIC to characterize the glycoproteome and phosphoproteome simultaneously. We also demonstrate that the ERLIC can be an alternative to the commonly used strong cation exchange chromatography for higher recovery of proteins during whole proteome analysis. These protocols can be easily adopted in most proteomics laboratories.

    Original languageEnglish (US)
    Title of host publicationNanoproteomics
    Subtitle of host publicationMethods and Protocols
    EditorsSteven Toms, Robert Weil
    Pages305-318
    Number of pages14
    DOIs
    StatePublished - Nov 10 2011

    Publication series

    NameMethods in Molecular Biology
    Volume790
    ISSN (Print)1064-3745

    Keywords

    • ERLIC
    • Glycoproteome
    • Mass spectrometry
    • Phosphoproteome
    • Proteome

    ASJC Scopus subject areas

    • Molecular Biology
    • Genetics

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