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J Am Soc Mass Spectrom. 2014 Mar;25(3):444-53. doi: 10.1007/s13361-013-0776-9. Epub 2014 Jan 3.

Structural documentation of glycan epitopes: sequential mass spectrometry and spectral matching.

Author information

1
Glycan Connections, LLC, Lee, NH, 03861, USA.

Abstract

Documenting mass spectral data is a fundamental aspect of accepted protocols. In this report, we contrast MS(n) sequential disassembly spectra obtained from natural and synthetic glycan epitopes. The epitopes considered are clusters found on conjugate termini of lipids and N- and O-glycans of proteins. The latter are most frequently pendant through a CID-labile HexNAc glycosidic linkage. The synthetic samples were supplied by collaborating colleagues and commercial sources and usually possessed a readily released reducing-end linker, a by-product of synthesis. All samples were comparably methylated, extracted, and MS(n) disassembled to compare their linkage and branching spectral details. Both sample types provide B-ion type fragments early in a disassembly pathway and their compositions are a suggestion of structure. Further steps of disassembly are necessary to confirm the details of linkage and branching. Included in this study were various Lewis and H antigens, 3- and 6-linked sialyl-lactosamine, NeuAc-2,8-NeuAc dimer, and Galα1,3Gal. Sample infusion provided high quality spectral data whereas disassembly to small fragments generates reproducible high signal/noise spectra for spectral matching. All samples were analyzed as sodium adducted positive ions. This study includes comparability statistics and evaluations on several mass spectrometers.

PMID:
24385394
PMCID:
PMC3950938
DOI:
10.1007/s13361-013-0776-9
[Indexed for MEDLINE]
Free PMC Article

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