Abstract
The two major sialoglycoproteins of the human erythrocyte membrane (α and δ, glycophorins A and B1,2) have identical amino acid sequences for the first 26 residues from the amino terminus, except that α expresses M or N blood group antigen activity whereas δ carries only blood group N activity. In addition, the asparagine at position 26 on α carries an oligosaccharide chain which is absent from the same position on δ. The two sialoglycoproteins differ in their remaining amino acid sequence and δ expresses blood group Ss activity. There are also variant sialoglycoproteins which have properties of both the α and δ molecules1,3 and may be hybrids of these. Using antibodies directed against different structural regions of the major sialoglycoprotein α, we confirm here that 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 α and δ. It is suggested that the two genes are closely associated in the order α, δ (5′ → 3′) on the chromosome.
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Mawby, W., Anstee, D. & Tanner, M. Immunochemical evidence for hybrid sialoglyco-proteins of human erythrocytes. Nature 291, 161–162 (1981). https://doi.org/10.1038/291161a0
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DOI: https://doi.org/10.1038/291161a0
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