Effect of modification of amino groups of human erythrocytes on M, N and NVg blood group specificities.
Modification of amino groups on the surface of human erythrocytes by acetic anhydride and trinitrobenzenesulfonic acid caused loss of agglutinability by human and rabbit anti-M and anti-N sera, was without any effect on agglutinability of N red cells by Vicia graminea agglutinin, and made M cells agglutinable by the same agglutinin. Modification of amino groups had no effect on agglutinability of red cells by anti-H and anti-A lectins and only slightly decreased agglutinability by human anti-H, anti-A and anti-I sera. The results suggest that the difference between M and N receptors is not determined by the structure of oligosaccharide chains.
D000812:Anhydrides / Q000494:pharmacology; D000818:Animals; D001789:Blood Group Antigens; D004912:Erythrocytes / Q000276:immunology*; D006384:Hemagglutination / Q000187:drug effects*; D006801:Humans; D007106:Immune Sera; D007518:Isoantibodies; D037102:Lectins; D009578:Nitrobenzenes / Q000494:pharmacology; D011817:Rabbits / Q000276:immunology; D013451:Sulfonic Acids / Q000494:pharmacology
D000812:Anhydrides; D001789:Blood Group Antigens; D007106:Immune Sera; D007518:Isoantibodies; D037102:Lectins; D009578:Nitrobenzenes; D013451:Sulfonic Acids