Method for characterizing sulfated glycoproteins in a glycosylation site-specific fashion, using ion pairing and tandem mass spectrometry.
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.
Department of Chemistry, University of Kansas, Lawrence, KS 66045, USA.
Janet
J
Irungu
Dilusha S
DS
Dalpathado
Eden P
EP
Go
Hui
H
Jiang
Hy-Vy
HV
Ha
George R
GR
Bousfield
Heather
H
Desaire
D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D007477:Ions; D013431:Sulfates / Q000737:chemistry*; D053719:Tandem Mass Spectrometry / Q000379:methods*
D006023:Glycoproteins; D007477:Ions; D013431:Sulfates