Abstract
N-glycans of a recombinant mouse soluble Fcγ receptor II (sFcγRII) expressed in baby hamster kidney cells were released from glycopeptides by digestion with glycoamidase A (from sweet almond), and the reducing ends of the oligosaccharides were reductively aminated with 2-aminopyridine. The derivatized N-glycans were separated and structurally identified by a three-dimensional high-performance liquid chromatography (HPLC) mapping technique on three kinds of HPLC columns [Takahashi, et al. (1995) Anal. Biochem. 226: 139–46]. Eighteen different major N-glycan structures were identified, of which six were neutral (45%), five mono-sialyl (49%), one di-sialyl (4.6%), five tri-sialyl (1.1%), and one tetra-sialyl (0.3%). All N-glycan structures determined were complex type with fucosylation at the N-acetylglucosamine residue of the reducing end, and N-acetylneuraminic acid, when present, was α-(2,3)-linked. The existence of a unique structure containing both N-acetylgalactosamine and α-(2,3)-N-acetylneuraminic acid residues at the reducing ends, as below, was confirmed by MALDI-TOF mass spectrometry.
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Takahashi, N., Yamada, W., Masuda, K. et al. N-glycan structures of a recombinant mouse soluble Fcγ receptor II. Glycoconj J 15, 905–914 (1998). https://doi.org/10.1023/A:1006915200989
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DOI: https://doi.org/10.1023/A:1006915200989