Journal
JOURNAL OF MASS SPECTROMETRY
Volume 45, Issue 5, Pages 528-535Publisher
WILEY
DOI: 10.1002/jms.1736
Keywords
N-Glycans; negative ion fragmentation; glycosylation disorder; MALDI; electrospray
Funding
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council
- Oxford Glycobiology Institute
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Negative ion CID spectra of N-linked glycans released from glycoproteins contain many ions that are diagnostic for specific structural features such as the detailed arrangement of antennae and the location of fucose residues. Identification of such ions requires reference glycans that are often difficult to acquire in a pure state. The recent acquisition of a sample of N-glycans from a patient lacking the enzyme N-acetylglucosaminyltransferase-2 provided an opportunity to investigate fragmentation of glycans lacking a 6-antenna. These glycans contained one or two galactose-N-acetylglucosamine-chains attached to the 3-linked mannose residue of the trimannosyl-chitobiose core with and without fucose substitution. The spectra from the patient sample clearly defined the antenna distribution and showed striking differences from the spectra of isomeric compounds obtained from normal subjects. Furthermore, they provided additional information on previously identified antenna-specific fragment ions and indicated the presence of additional ions that were diagnostic of fucose substitution. Glycans obtained from such enzyme-deficient patients can, thus, be a valuable way of obtaining spectra of specific isomers in a relatively pure state for interpretation of mass spectra. Copyright (C) 2010 John Wiley & Sons, Ltd.
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