Abstract
Abstract Binding isotherms of a local anesthetic, dibucaine, to phospholipid vesicles were measured using a dialysis method. Two types of phospholipids, dilauroylphosphatidic acid (DLPA) and dilauroylphosphatidylcholine (DLPC), were used to prepare vesicles. The binding isotherms for pure DLPA and DLPC vesicles and their mixtures were analyzed with the Hill equation. The binding parameters obtained for pure phospholipid vesicles reproduce the binding isotherms for the mixed vesicles by taking account of the mixing ratio; this indicates the presence of independent binding sites, corresponding to the DLPA and DLPC molecule, in the mixed vesicle.
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