Heat-induced Electrophoretic Anomalies of Red Cell Membrane Nonsialoglycoproteins

Abstract

The effects of heating at 100° in the presence and absence of dithiothreitol has been examined in SDS-solubilized ghost membranes and isolated integral membrane proteins from human red cells. A significant increase in electrophoretic mobility and broadening of the major polypeptide band 3 was found. The anomalous behavior of band 3 alone could explain the apparent disappearance of band 4 which has occasionally been reported in hereditary spherocytosis red cells.