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Mass spectrometry in the analysis of N-linked and O-linked glycans
Mass spectrometry (MS) continues to play a vital role in defining the structures of N-glycans and O-glycans in glycoproteins via glycomic and glycoproteomic methodologies. The former seeks to define the total N-glycan and/or O-glycan repertoire in a biological sample whilst the latter is concerned w...
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Published in: | Current opinion in structural biology 2009-10, Vol.19 (5), p.498-506 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | Mass spectrometry (MS) continues to play a vital role in defining the structures of
N-glycans and
O-glycans in glycoproteins via glycomic and glycoproteomic methodologies. The former seeks to define the total
N-glycan and/or
O-glycan repertoire in a biological sample whilst the latter is concerned with the analysis of glycopeptides. Recent technical developments have included improvements in tandem mass spectrometry (MS/MS and MS
n) sequencing methodologies, more sensitive methods for analysing sulfated and polysialylated glycans and better procedures for defining the sites of
O-glycosylation. New tools have been introduced to assist data handling and publicly accessible databases are being populated with glycomics data. Progress is exemplified by recent research in the fields of glycoimmunology, reproductive glycobiology, stem cells, bacterial glycosylation and non-mucin
O-glycosylation. |
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ISSN: | 0959-440X 1879-033X |
DOI: | 10.1016/j.sbi.2009.05.005 |