期刊
ANALYTICAL AND BIOANALYTICAL CHEMISTRY
卷 399, 期 10, 页码 3359-3365出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s00216-011-4652-9
关键词
Click OEG-CD; Glycopeptide enrichment; Glycoproteomics; Hydrophilic interaction liquid chromatography
资金
- National Natural Science Funds for Distinguished Young Scholar [20825518]
- National Science Foundation of China [20805046]
- Chinese Academy of Sciences [KSCX2-YW-R-170]
Selective enrichment of glycopeptides is of great importance for protein glycosylation analysis using mass spectrometry since the signals of glycopeptides could be severely suppressed by the coexisting non-glycosylated peptides in the protein digest. In the present work, a strategy for N-linked glycopeptide enrichment through reversed-phase depletion coupled with hydrophilic affinity enrichment by applying the customized matrix named Click OEG-CD is developed. Compared with single hydrophilic interaction liquid chromatography (HILIC) mode, the strategy exhibited remarkably higher selectivity for N-linked glycopeptides. As many as 22, 18, and eight glycopeptides were detected in the glycopeptide fraction enriched with the strategy from the digests of human immunoglobulin G, horseradish peroxidase and bovine ribonuclease B, respectively. In addition, the strategy also showed high glycosylation microheterogeneity coverage for the enrichment of human alpha(1)-acid glycoprotein glycopeptides. More than 170 glycopeptides covering all the glycosylation sites were detected in the enriched fraction. The revered-phase liquid chromatography depletion coupled with HILIC enrichment strategy by using Click OEG-CD matrix is expected to show more potential in further applications in glycosylation analysis.
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