title: Structural properties of the human MN blood group antigen receptor sites.
abstract: It is shown that the MN blood group antigen determinant of the major human erythrocyte membrane (MN) sialoglycoprotein is located on its N-terminal octaglycopeptide. The only analytically detectable difference between peptides from MM and NN cells are Ser/Leu and Gly/Glu polymorphisms at the first and fifth positions, respectively. Destruction of the antigens by removal of the N-terminal residues suggests that these amino acids represent a part of the receptor areas for various anti-M or -N reagents. Evidence is presented that the N-terminal structure of the Ss glycoprotein is identical with that of MN glycoprotein from NN red cells up to the fifth residue. This provides an explanation for the 'N' antigen on this molecule and direct support for the earlier proposal that the MNSs locus is represented by homologous genes.
mesh_terms: D001666:Binding Sites, Antibody; D000939:Epitopes; D004910:Erythrocyte Membrane / Q000276:immunology; D006021:Glycophorins / Q000276:immunology*; D006801:Humans; D008951:MNSs Blood-Group System; D012795:Sialoglycoproteins / Q000276:immunology* / Q000302:isolation & purification
chemical_list: D000939:Epitopes; D006021:Glycophorins; D008951:MNSs Blood-Group System; D012795:Sialoglycoproteins