Permethylation and tandem mass spectrometry of oligosaccharides having free hexosamine: analysis of the glycoinositol phospholipid anchor glycan from the scrapie prion protein.
Permethylation of the glycan isolated from the glycoinositol phospholipid (GPI) anchor of the scrapie prion protein (PrPSc) trimethylates a free hexosamine to form a quarternary ammonium salt, substantially increasing the sensitivity for analysis by mass spectrometry. This derivatization induces specific fragmentation reactions in collision-induced dissociation spectra obtained on a four-sector tandem mass spectrometer, identifying the branching pattern of the PrPSc GPI glycan.
Baldwin
M A
MA
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143.
Stahl
N
N
Reinders
L G
LG
Gibson
B W
BW
Prusiner
S B
SB
Burlingame
A L
AL
D006017:Glycolipids / Q000032:analysis*; D017261:Glycosylphosphatidylinositols; D006595:Hexosamines / Q000737:chemistry*; D008745:Methylation; D015394:Molecular Structure; D009844:Oligosaccharides / Q000737:chemistry*; D010716:Phosphatidylinositols / Q000032:analysis*; D018620:PrPSc Proteins; D011328:Prions / Q000032:analysis*; D013057:Spectrum Analysis; D014764:Viral Proteins / Q000032:analysis* / Q000737:chemistry
D006017:Glycolipids; D017261:Glycosylphosphatidylinositols; D006595:Hexosamines; D009844:Oligosaccharides; D010716:Phosphatidylinositols; D018620:PrPSc Proteins; D011328:Prions; D014764:Viral Proteins