Recent advances in methods for the analysis of protein o‐glycosylation at proteome level

Skip to Navigation

EarlyView Article

  • Published: Nov 2, 2017
  • Author: Xin You, Hongqiang Qin, Mingliang Ye
  • Journal: Journal of Separation Science


O‐Glycosylation, which refers to the glycosylation of the hydroxyl group of side chains of Serine/Threonine/Tyrosine residues, is one of the most common post‐translational modifications. Compared with N‐linked glycosylation, O‐glycosylation is less explored because of its complex structure and relatively low abundance. Recently, O‐glycosylation has drawn more and more attention for its various functions in many sophisticated biological processes. To obtain a deep understanding of O‐glycosylation, many efforts have been devoted to develop effective strategies to analyze the two most abundant types of O‐glycosylation, i.e. ON‐acetylgalactosamine and ON‐acetylglucosamine glycosylation. In this review, we summarize the proteomics workflows to analyze these two types of O‐glycosylation. For the large‐scale analysis of mucin‐type glycosylation, the glycan simplification strategies including the ‘‘SimpleCell’’ technology were introduced. A variety of enrichment methods including lectin affinity chromatography, hydrophilic interaction chromatography, hydrazide chemistry, and chemoenzymatic method were introduced for the proteomics analysis of ON‐acetylgalactosamine and ON‐acetylglucosamine glycosylation.

Social Links

Share This Links

Bookmark and Share


Suppliers Selection
Societies Selection

Banner Ad

Click here to see
all job opportunities

Most Viewed

Copyright Information

Interested in spectroscopy? Visit our sister site

Copyright © 2017 John Wiley & Sons, Inc. All Rights Reserved