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- W2088124549 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 α- and β-chains. Two structurally distinct glycosylation patterns were detected for the α-chain species, the α1 with high-mannoseand complex-type oligosaccharides and α2 with a complex-type one. In contrast, the β-chain species contains only complex-type oligosaccharides. Further oligosaccharide heterogeneity is found for each α1-, α2- and β-chain described. In contrast to murine and guinea-pig la antigens, no significant amount of glycopeptides with biantennary structure was found in HLA-DR." @default.
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- W2088124549 date "1985-09-01" @default.
- W2088124549 modified "2023-09-27" @default.
- W2088124549 title "Analysis of HLA-DR antigen glycosylation by serial lectin affinity chromatography" @default.
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- W2088124549 doi "https://doi.org/10.1016/0161-5890(85)90108-7" @default.
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