Analysis of normal human tonsil class II antigen glycosylation by lectin affinity chromatography.
Human class II molecules include the HLA-DR, -DQ, and -DP alloantigens. Each class II molecule consists of two glycosylated polypeptide chains, the alpha chain and the beta chain. We have used lectin affinity analysis to investigate the glycosylation pattern of [3H]mannose-labeled glycopeptides derived from isolated alpha and beta chains of HLA-DR and -DQ molecules of normal tonsil cells. Glycopeptides obtained by Pronase digestion of each isolated chain were passed sequentially over columns of immobilized concanavalin A, Lens culinaris lectin, and phytohemagglutinins E and L in a prescribed manner to generate a lectin affinity profile which could be used to assign a minimal oligosaccharide structure for each glycopeptide studied. The data presented here demonstrate that a given class II polypeptide chain can bear several different oligosaccharides. Comparison of the glycosylation patterns of the HLA-DR and -DQ molecules shows that they are similar in most respects. However, there are qualitative differences in the oligosaccharides borne by HLA-DQ and -DR molecules. In addition, comparison between HLA-DQ and the homologous murine I-A molecules shows species-specific glycosylation patterns.[1]References
- Analysis of normal human tonsil class II antigen glycosylation by lectin affinity chromatography. Zacheis, M., Giacoletto, K., Schwartz, B.D. J. Biol. Chem. (1986) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
