Structural characterization of the oligosaccharides of a human monoclonal anti-lipopolysaccharide immunoglobulin M |
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Authors: | Leibiger H; Kersten B; Albersheim P; Darvill A |
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Institution: | Complex Carbohydrate Research Center, University of Georgia, Athens 30602-4712, USA. |
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Abstract: | The oligosaccharide side chains of a human anti-lipopolysaccharide IgM
produced by a human-human-mouse heterohybridoma were analyzed at each of
its five conserved N-glycosylation sites. This antibody also has a
potential sixth N-glycosylation site in the variable region of its heavy
chain which is not glycosylated. The oligosaccharides were released by
digestion with various endo- and exoglycosidases and analyzed by
matrix-assisted laser desorption/ionization-time of flight mass
spectrometry and fluorophore-assisted carbohydrate electrophoresis. The
antibody has various complex- and hybrid-type oligosaccharide structures at
Asn 171, various sialylated complex-type oligosaccharides at Asn 332 and
395, and high-mannose-type oligosaccharides at Asn 402 and 563. Of note is
the presence in this human IgM of oligosaccharides containing
N-glycolylneuraminic acid and N-acetylneuraminic acid in the ratio of 98:2
as determined using anion- exchange chromatography. Furthermore, we
observed oligosaccharide structures containing Gal alpha (1,3)Gal that have
not been reported as components of human glycoproteins.
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