On the mechanism of transport of salicylate and p-hydroxybenzoic acid across human red cell membranes.
The pH-dependence of efflux of salicylate and p-hydroxybenzoic acid (PHB) from human red cells indicates that the un-ionized species penetrates the membrane. No effect of the anion channel blocker 4,4'-diisothiocyano-2,2'-disulphonic stilbene was observed. The temperature-dependence of efflux suggests that the energy barrier to transport of salicylate and PHB is the transfer of the acids from water into the membrane, rather than transport through the membrane interior. Intracellular binding of both acids was found to be pH-dependent.
D001692:Biological Transport; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D062385:Hydroxybenzoates / Q000378:metabolism*; D066298:In Vitro Techniques; D007700:Kinetics; D010226:Parabens; D000091402:Prohibitins; D012459:Salicylates / Q000378:metabolism*; D013696:Temperature
D062385:Hydroxybenzoates; C000717328:PHB protein, human; D010226:Parabens; D000091402:Prohibitins; D012459:Salicylates; C038193:4-hydroxybenzoic acid