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Liquid chromatography-tandem mass spectrometry-based fragmentation analysis of glycopeptides
The use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS n ) for the glycoproteomic characterization of glycopeptides is a growing field of research. The N- and O-glycosylated peptides (N- and O-glycopeptides) analyzed typically originate from protease-digested gl...
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Published in: | Glycoconjugate journal 2016-06, Vol.33 (3), p.261-272 |
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Main Author: | |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The use of liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS
n
) for the glycoproteomic characterization of glycopeptides is a growing field of research. The N- and O-glycosylated peptides (N- and O-glycopeptides) analyzed typically originate from protease-digested glycoproteins where many of them are expected to be biomedically important. Examples of LC-MS
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and MS
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fragmentation strategies used to pursue glycan structure, peptide identity and attachment-site identification analyses of glycopeptides are described in this review. MS
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spectra, using the CID and HCD fragmentation techniques of a complex biantennary N-glycopeptide and a core 1 O-glycopeptide, representing two examples of commonly studied glycopeptide types, are presented. A few practical tips for accomplishing glycopeptide analysis using reversed-phase LC-MS
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shotgun proteomics settings, together with references to the latest glycoproteomic studies, are presented. |
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ISSN: | 0282-0080 1573-4986 |
DOI: | 10.1007/s10719-016-9649-3 |