For the purpose of clarifying the action of procaine physically or molecularly, the pattern of association or dissociation of the surface-bound Ca
++ was isotopically investigated when procaine was applied externally. It was presumed that procaine acted in a cationic form and the results were compatible with an interaction of procaine with anionic sites on the membrane.1) The effect of local anesthetics might not be established through the change in membrane potential level, and external Ca ions had no relation to an interaction between these two parameters. Procaine immobilized
45Cakinetics on the membrane surface. During the time of Ca
++ immobilization, exchange diffusion of Na ions was stimulated. The immobilizing action of procaine took place regardless of the presence of external Ca ions.2) Procaine acted probably on a protein portion of the membrane, but it was suggested that for this activity the maintenance of an assembly of membrane lipoprotein was required. It was negligible to consider lipoprotein-calcium-procaine complex formation in the membrane. The anionic sites for procaine may locate in a protein portion but are not identical with the sites proper to Ca ions. Procaine and Ca ions do probably not compete for the same site on the membrane components.3) It is supposed from the results that the selective binding of procaine to lipoprotein, particularly to its protein portion and not to original Ca sites, inhibits secondarily an exchangeability of Ca ions preferentially bound to protein by means of induction in a physical sense.
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