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The oligosaccharide units of rabbit immunoglobulin G. Multiple carbohydrate attachment sites.

ABSTRACT: The carbohydrate structure of rabbit immunoglobulin G isolated from pooled sera was investigated. Amino sugar analysis of fragments of the molecule allowed three oligosaccharides to be located at separate sites on the H-chain. The corresponding glycopeptides were isolated. The average composition of the C1-oligosaccharide was 2 glucosamine, 1 mannose and 2 galactose residues. It appeared to be present in approx. 15% of the H-chains; the carbohydrate was coupled through the amide group of asparagine in a peptide containing asparagine, glycine and threonine within the Fd fragment of the molecule. The average composition of the C2-oligosaccharide was 1 galactosamine, 1 galactose and either 1 or 2 sialic acid residues. It was present on approx. 40% of the H-chains and was attached glycosidically to the OH group of threonine in a peptide Ser-Lys-Pro-Thr-Cys-Pro-Pro-Glu-Leu in the hinge region of the molecule. The average composition of the C3-oligosaccharide was 5 glucosamine, 2 galactose, 5 mannose, 1 fucose and 1 sialic acid residue. It appeared to be present in all the H-chains and was linked through the amide group of asparagine in a peptide Gln-Gln-Phe-Asn-Ser-Thr-Ile-Arg within the Fc fragment of the molecule.

SUBMITTER: Fanger MW

PROVIDER: S-EPMC1178785 | biostudies-other | 1972 May

REPOSITORIES: biostudies-other

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The oligosaccharide units of rabbit immunoglobulin G. Asymmetric attachment of C2-oligosaccharide.

Project description:Two populations of immunoglobulin G (IgG) molecules were isolated from pooled rabbit serum. The first was almost devoid of galactosamine and was obtained in a yield of 7% of the total IgG; the second contained on average a single residue of galactosamine per molecule and was obtained in a yield of 30% of the total IgG. The galactosamine, which is present solely in the C2-oligosaccharide, appeared to be present on one H-chain and not the other in the four-chain structure. Evidence was obtained by the isolation of a glycopeptide linked through a disulphide bridge to a second peptide of the same sequence; the oligosaccharide attached to the first peptide was absent from the complementary peptide. Further evidence was obtained by degradation and analysis of the 5S IgG fragment, which comprises an intact half-molecule coupled through a disulphide bridge to the Fc fragment derived from the opposing half molecule (Goodman, 1965); only the intact H-chain carried the C2-oligosaccharide.

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