Comparison of Enrichment Methods for Intact N- and O-Linked Glycopeptides Using Strong Anion Exchange and Hydrophilic Interaction Liquid Chromatography.

ABSTRACT: Heterogeneity of protein glycosylation poses great challenges for analysis that is key to understand structure and function of glycoproteins. Resolving this conundrum requires efficient and specific enrichment of intact glycopeptides for identification and quantitation. To this end, hydrophilic interaction chromatography (HILIC) has been commonly used to enrich intact N- and O-linked glycopeptides. However, its effectiveness to enrich isobarically labeled glycopeptides remains unclear. Here, we studied three different enrichment methods for enrichment of N- and O-linked glycopeptides. It was found that removal of N-glycans prior to enrichment of O-linked glycopeptides by HILIC improved identification of O-linked glycopeptides by mass spectrometry. We also compared the enrichment of intact

SUBMITTER: Yang W 

PROVIDER: S-EPMC5850954 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature