The 'hollow cylinder' protein of erythrocyte membranes

The 'hollow cylinder' protein (Harris, J.R. (1968) Biochim. Biophys. Acta 150, 534-537) has been purified from human erythrocyte membranes. The molecular weight of the native protein, as determined by analytical ultracentrifugation, was found to be 747,000. By means of sodium dodecyl sulphate gel electrophoresis, the purified protein was shown to be composed of three different low molecular weight polypeptides of average molecular weight 25,000. This study provides convincing evidence that the spectrin tetramer is not responsible for the characteristic electron microscopic appearance of the hollow cylinder protein.