FATTY ACYLATION OF A 55 KDA MEMBRANE-PROTEIN OF HUMAN ERYTHROCYTES

The major palmitoylated human erythrocyte membrane protein has an M(r) of 55 000. It is distinct from the glucose transporter and is not derived from band 3 or ankyrin. It resists salt extraction suggesting a high affinity for the membrane. Pulse chase experiments demonstrate that palmitoylation is a dynamic process, and it may therefore have regulatory significance in membrane protein-protein or protein-lipid interaction. Slower dynamics of palmitoylation in erythrocytes from patients suffering from chronic myelogenous leukemia, which are less stable than normal erythrocytes, strengthen this view.