Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum.

ABSTRACT: The lack of consensus sequence, common core structure, and universal endoglycosidase for the release of O-linked oligosaccharides makes O-glycosylation more difficult to tackle than N-glycosylation. Structural elucidation by mass spectrometry is usually inconclusive as the CID spectra of most glycopeptides are dominated by carbohydrate-related fragments, preventing peptide identification. In addition, O-linked structures also undergo a gas-phase rearrangement reaction, which eliminates the sugar without leaving a telltale sign at its former attachment site. In the present study we report the enrichment and mass spectrometric analysis of proteins from bovine serum bearing Galbeta1-3GalNAcalpha (mucin core-1 type) structures and the analysis of O-linked glycopeptides utilizing electron trans

SUBMITTER: Darula Z 

PROVIDER: S-EPMC2773718 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature