Studies on the membrane glycoprotein defect of En(a-) erythrocytes. III. N-terminal amino acids of sialoglycoproteins from normal and En(a-) red cells

Abstract

Sodium dodecylsulphate polyacrylamide gel electrophoretic methods and quantitative analyses of the N-terminal amino acids were applied to the sialoglycoprotein mixture and glycoprotein fractions from normal erythrocyte membranes, as well as preparations from red cells of individuals belonging to the English and Finnish En(a-) families. The data confirm the observation by alternative methods that SS cells exhibit a higher Ss glycoprotein content than ss erythrocytes. The results of end-group analyses suggest that the N-terminal amino acids serine and leucine represent the structures differentiating the MN and the 'M' and 'N' antigens on the MN and Ss glycoproteins respectively. Data from peptide sequence analyses confirm that the glycine/glutamic acid polymorphism at the fifth position of the MN glycoprotein's peptide chain is closely or absolutely linked with the serine/leucine polymorphism at its N-terminal position. As normal (EnaEna) red cells exhibiting 'M' antigenic properties have not been detected, the hypothesis is proposed that the Ss glycoprotein of English En(a-) erythrocytes possesses an MN-Ss hybrid polypeptide chain analogous to those of the delta-beta Lepore haemoglobins.