Journal
PROTEOMICS
Volume 16, Issue 2, Pages 241-256Publisher
WILEY
DOI: 10.1002/pmic.201500266
Keywords
Glycomics; Glycoproteomics; iGIG; Isobaric labeling; Mass spectrometry
Funding
- National Institutes of Health, National Heart Lung and Blood Institute
- Johns Hopkins Proteomics Center [N01-HV-00240]
- Programs of Excellence in Glycosicences (PEG) [P01HL107153]
- National Institutes of Health, National Cancer Institute
- Early Detection Research Network (EDRN) [U01CA152813]
- Clinical Proteomic Tumor Analysis Consortium (CPTAC) [U24CA160036]
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Over the past decade, considerable progress has been made with respect to the analytical methods for analysis of glycans from biological sources. Regardless of the specific methods that are used, glycan analysis includes isolation, identification, and quantitation. Derivatization is indispensable to increase their identification. Derivatization of glycans can be performed by permethylation or carbodiimide coupling/esterification. By introducing a fluorophore or chromophore at their reducing end, glycans can be separated by electrophoresis or chromatography. The fluorogenically labeled glycans can be quantitated using fluorescent detection. The recently developed approaches using solid-phase such as glycoprotein immobilization for glycan extraction and on-tissue glycan mass spectrometry imaging demonstrate advantages over methods performed in solution. Derivatization of sialic acids is favorably implemented on the solid support using carbodiimide coupling, and the released glycans can be further modified at the reducing end or permethylated for quantitative analysis. In this review, methods for glycan isolation, identification, and quantitation are discussed.
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