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  • Title: Analysis of HLA-DR antigen glycosylation by serial lectin affinity chromatography.
    Author: Neel D, Giner M, Merlu B, Turmel P, Goussault Y, Charron DJ.
    Journal: Mol Immunol; 1985 Sep; 22(9):1053-9. PubMed ID: 3865052.
    Abstract:
    The structure of the N-linked oligosaccharides of HLA-DR molecules from an HLA-DR homozygous B-lymphoblastoid cell line (CA) was characterized by serial lectin affinity analysis. Glycans lectin affinity profile were obtained for the HLA-DR complex and separated alpha- and beta-chains. Two structurally distinct glycosylation patterns were detected for the alpha-chain species, the alpha 1 with high-mannose- and complex-type oligosaccharides and alpha 2 with a complex-type one. In contrast, the beta-chain species contains only complex-type oligosaccharides. Further oligosaccharide heterogeneity is found for each alpha 1-, alpha 2- and beta-chain described. In contrast to murine and guinea-pig Ia antigens, no significant amount of glycopeptides with biantennary structure was found in HLA-DR.
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