Primary structure of a small glycopeptide isolated from human glomerular basement membrane and carrying a major antigenic site.

作者: Philippe M. Mahieu , Guy R. Maghuin-Rogister , Paul H. Lambert

DOI: 10.1111/J.1432-1033.1973.TB03232.X

关键词:

摘要: The glycopeptides containing either the disaccharide or heteropolysaccharide chains were purified, after enzymatic digestion of glomerular basement-membrane antigens, by gel filtration and ion-exchange chromatography. Their antigenicity was investigated in seven patients with anti-glomerular-basement-membrane antibody-mediated glomerulonephritis, leukocyte migration test radioimmunoassay. The is inhibited presence membrane antigens both types oligosaccharide chains. disaccharide-containing glycopeptide inhibits these using 10-times less antigenic material; heteropolysaccharide-containing does not modify leudkocyte same patients. Similarly, only decreases binding labelled antibodies, radioimmunoassay. This carries therefore major determinants humoral cellular anti-basement-membrane auto-immunization. The amino acid sequence Hyl-Gly-Glu-Asp-Gly, prosthetic group being linked to hydrolysine residue peptidic chain; its immunodominant site formed Galp-Hyl unit.

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