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The study of glycoproteins as intact molecules or as smaller fragments generated by chemical or enzymatic digestion is wellsuited to the technique of capillary zone electrophoresis-electrospray mass spectrometry (CZE-ESMS). Separation of glycoformpopulations of intact glycoproteins or protein digests is possible using buffers compatible with mass spectrometric detection(
1
–
8
). CZE-ESMS analysis of intact proteins can provide semiquantitative information about the degree of heterogeneity of theglycoprotein (
1
,
6
,
7
). Enzymatic or chemical digestion of the glycoprotein, followed by CZE-ESMS, gives a direct measure of individual sites ofheterogeneity (
1
–
5
). Combined CZE-collision induced dissociation (CID) mass spectrometric experiments (CZE-MS-MS) of digests enables the characterizationof oligosaccharide structures (
1
–
5
). In particular, CID of glycopeptides is characterized by fragment ions corresponding to cleavage at each glycosidic bond. The occurrence of specific carbohydrate residues such as hexose (Man, Glc, Gal),
N
-acetylhexosamine (GlcNAc, GalNAc), or N-acetylneuraminic acid (NeuNAc) can be monitored by the observation of characteristicoxonium ions at
m/z
163, 204, and 292, respectively. More recently, CZE-front-end CID-MS-MS has been shown to be a powerful tool for peptidesequencing of glycopeptides using subpicomole quantities of injected glycoprotein (
3
–
5
).