Immunochemical evidence for hybrid sialoglycoproteins of human erythrocytes.

Abstract

The two major sialoglycoproteins of the human erythrocyte membrane (alpha and delta, glycophorins A and B) have identical amino acid sequences for the first 26 residues from the amino terminus, except that alpha expresses M or N blood group antigen activity whereas deta carries only blood group N activity. In addition, the asparagine at position 26 on alpha carries an oligosaccharide chain which is absent from the same position on delta. The two sialoglycoproteins differ in their remaining amino acid sequence and delta expresses blood group Ss activity. There are also variant sialoglycoproteins which have properties of both the alpha and delta molecules and may be hybrids of these. Using antibodies directed against different structural regions of the major sialoglycoprotein alpha, we confirm here and two variant erythrocytes (Miltenberger class V (MiV) and Ph) contain hybrid sialoglycoprotein molecules (Fig. 1). These hybrid sialoglycoproteins arise from cross-over events between the genes coding for alpha and delta. It is suggested that the two genes are closely associated in the order alpha, delta (5' leads to 3') on the chromosome.