Abstract
The membrane of En(a-) human erythrocytes were as part of a study of the structure and biochemical function of the surface [antigen] glycoproteins of the mammalian cell. En(a-) erythrocytes were selected because they have more extensive changes at the cell surface than any other known erythrocyte variant. In En(a-) erythrocytes, the major membrane sialoglycoprotein is lacking, and the other major membrane-penetrating glycoprotein (band 3) has an altered electrophoretic mobility. The apparent clinical normality of En(a-) cells suggests that the change in band 3 may compensate for the loss of the membrane sialoglycoprotein. A viable erythrocyte can exist despite the absence of one of its major surface components.