doi: 10.1016/0003-2697(90)90405-x.
Permethylation and tandem mass spectrometry of oligosaccharides having free hexosamine: analysis of the glycoinositol phospholipid anchor glycan from the scrapie prion protein
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- PMID: 1981823
- DOI: 10.1016/0003-2697(90)90405-x
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Permethylation and tandem mass spectrometry of oligosaccharides having free hexosamine: analysis of the glycoinositol phospholipid anchor glycan from the scrapie prion protein
Anal Biochem.
.
Abstract
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.
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