The polypeptides of the human erythrocyte membrane were analyzed by polyacrylamide gel electrophoresis in 1 % sodium dodecyl sulfate. Six major bands (I-VI) together make up over two-thirds of the protein staining profile. Component III (mol wt 89,000) predominates in the ghost membrane; it constitutes 30% of the protein and numbers over 106 chains/ghost. Components I and II form a slow-moving doublet (approximate mol wt 250,000) containing 25 % of the protein. The molar amounts of I + II, IV (mol wt 77,500),

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Plasma membranes purified from human red cells were Converted into small vesicleS by disruption in alkaline buffer of low ionic strength. Most of these vesicles were inside-out. The presence of divalent cations prevented this inversion. The inside-out vesicles were separatcd from right-side-out vesicles by centrifugration to equilibrium in dextran density gradients.