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Large-Scale Identification and Fragmentation Pathways Analysis of N-Glycans from Mouse Brain.
- Source :
-
Journal of the American Society for Mass Spectrometry . Jul2019, Vol. 30 Issue 7, p1254-1261. 8p. - Publication Year :
- 2019
-
Abstract
- N-linked glycosylation is one of the most common protein PTMs, and the topological structure (monosaccharide composition and sequence as well as glycosidic linkages) of N-glycans is vital information to understand their biological functions and roles. Tandem mass spectrometry has been widely used for topological structure characterization of N-glycans, where comprehensive understanding of fragmentation pathways and characteristics of product ions are essential to achieve best interpretation of MS/MS data and highest confidence of identification. Here, we report our glycomic study of N-glycome of mouse brain as well as fragmentation pathway analysis of the identified N-glycans. With LC-MS/MS analysis at both the positive and negative ESI modes together with our recently developed N-glycan database search engine GlySeeker, 221 unique N-glycans with putative topological structures were identified with target-decoy searches and number of best hits of 1. Analysis of fragmentation pathways and characteristics of product ions of permethylated N-glycans in the positive mode and native N-glycans in the negative mode were further carried out. The reported N-glycans serve as a basic reference for future glycosylation study of mouse brain; and in general database search of tandem mass spectra of N-glycans, B/Y/Z ions should be preferentially considered for the permethylated form in the positive mode and B/C/Z ions for the native form in the negative mode. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10440305
- Volume :
- 30
- Issue :
- 7
- Database :
- Academic Search Index
- Journal :
- Journal of the American Society for Mass Spectrometry
- Publication Type :
- Academic Journal
- Accession number :
- 137147920
- Full Text :
- https://doi.org/10.1007/s13361-019-02181-y