Characterization of Glycan Binding Site of O-Linked Glycopeptides Using MALDI-7090 High-Resolution MALDI-TOF MS

The majority of proteins synthesized in biological organisms undergo glycosylation. Glycosylation is modification with glycans of high structural heterogeneity composed of multiple monosaccharides, such as glucose and galactose, which are bonded together. These glycans classified into N-linked types and O-linked types. These types of glycan are known to play an important role in regulating protein function, and obtaining information on protein glycosylation is essential to the development of biopharmaceuticals. In this article, we present a method for determining the O-linked glycan binding site that uses partial digestion with multiple enzymes and the MALDI-7090 high resolution MALDI-TOF MS.