Abstract
We have used tandem mass spectrometry (MS/MS)-based analysis of glycopeptides in order to identify the composition and structure of rare glycoforms. The results illustrate utility of low-energy MS/MS for structure identification. We have shown the presence of bifucosylated and trifucosylated glycoforms in human α-1-acid glycoprotein (AGP), a major plasma glycoprotein. Fucosylation in the case of AGP always occurs on the antennae; core fucosylation was not observed.
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