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Abstract
Precise and rapid glyco-mapping of a mouse monoclonal immunoglobulin G2b (IgG2b) was carried out by liquid chromatography-electrospray ionization ion trap-mass spectrometry/mass spectrometry (LC/ESI IT-MS/MS). It was possible to obtain spectra of minor glycopeptides with a quantity as low as 1.8 pmol. Reduced and carboxymethylated mouse antidansyl monoclonal IgG2b (RCM-IgG2b) was digested with Lys-C. Proteolytic peptides were subjected to capillary HPLC separation followed by analysis with an ion trap mass spectrometer. The structures of twelve different types of O-linked oligosaccharides attached to Thr-221AH in the hinge region and those of three major types of N-linked oligosaccharides attached to Asn-297H have been characterized.
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