Abstract
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.
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