The binding of chlorpromazine and its quaternary analogue chlorpromazine methoiodide to open and resealed human erythrocyte ghost membranes was studied. The results were compared with binding to liposomes of phosphatidylcholine or phosphatidylcholine with phosphatidylserine. The results indicate that the quaternary compound is confined to the outside face of the membrane. For both compounds two classes of binding sites are available. The strongest binding sites are mainly located on the inner surface of the membrane. The binding data suggest an asymmetric distribution of chlorpromazine in the membrane. © 1977.
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