An immunochemical study on anti-N antibodies from dialysis patients.
The specificity of anti-N antibodies from dialysis patients was investigated by hemagglutination in-hibition tests, using various fractionation, fragmentation and modification products of human erythrocytic membrane sialoglycoproteins. The antibodies were found to react with the N and "N' antigens on the MN and Ss glycoprotein, respectively. The NH2-terminal leucine and the side chain(s) of sialic acid(s) in oligosaccharide(s) linked to the second, third and/or fourth position(s) of the glycoproteins represent parts of the binding site for the anti-N antibodies. Formaldehyde reacts with the amino group of the NH2-terminal leucine, presumably leading to the formation of the hydroxy-methylene-derivative. These modified N antigens represent the structures triggering the formation of anti-N antibodies in dialysis patients, which cross-react with the native N receptors.
D000818:Animals; D000906:Antibodies; D005557:Formaldehyde / Q000494:pharmacology; D006020:Glycopeptides / Q000276:immunology / Q000494:pharmacology; D006023:Glycoproteins / Q000494:pharmacology; D006385:Hemagglutination Inhibition Tests; D006801:Humans; D008951:MNSs Blood-Group System / Q000276:immunology*; D011817:Rabbits; D006435:Renal Dialysis; D012794:Sialic Acids / Q000378:metabolism; D012795:Sialoglycoproteins / Q000276:immunology / Q000494:pharmacology
D000906:Antibodies; D006020:Glycopeptides; D006023:Glycoproteins; D008951:MNSs Blood-Group System; D012794:Sialic Acids; D012795:Sialoglycoproteins; D005557:Formaldehyde