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
PublisherHumana Press Inc.
Pages305-318
Number of pages14
ISBN (Print)9781617793189
DOIs
StatePublished - 2011

Publication series

NameMethods in Molecular Biology
Volume790
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • ERLIC
  • Glycoproteome
  • Mass spectrometry
  • Phosphoproteome
  • Proteome

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this