| Autor: |
Zacheis, M, Giacoletto, K, Schwartz, B D |
| Zdroj: |
Journal of Biological Chemistry; December 1986, Vol. 261 Issue: 36 p17004-17010, 7p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
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