Method for characterizing sulfated glycoproteins in a glycosylation site-specific fashion, using ion pairing and tandem mass spectrometry
Dalpathado, Dilusha S.
Go, Eden P.
Bousfield, George R.
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Janet Irungu, Dilusha S Dalpathado, Eden P Go, Hui Jiang, Hy-Vy Ha, George R Bousfield, Heather Desaire; Method for Characterizing Sulfated Glycoproteins in a Glycosylation Site-Specific Fashion, Using Ion Pairing and Tandem Mass Spectrometry; Anal. Chem., 2006, 78 (4), pp 1181–1190 DOI: 10.1021/ac051554t
Structural analysis of sulfated glycans is essential in understanding their biological significance. Here, we present a new approach to characterize sulfated glycans present on glycoproteins. The analysis is performed on glycopeptides, so information about the sulfated species is obtained in a glycosylation site-specific manner. This method employs an ion-pairing reagent to stabilize the SO3 group of the glycopeptide, allowing useful information to be obtained during MS/MS experiments. The amount of structural information obtained from (+)ESI-MS/MS of the ion-pair complexes for sulfated glycopeptides of equine thyroid stimulating hormone is compared with information obtained by (−)ESI-MS/MS of the underivatized, sulfated glycopeptides. The results indicate that this new method provides detailed insights into the sequence, branching, and type of N-glycans present, compared to analysis via (−)ESI-MS/MS.
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