Transmembrane electrophoresis of 8-anilino-1-naphthalenesulfonate through egg lecithin liposome membranes.
Valinomycin has been shown to increase the amount of 8-anilino-1-naphthalenesulfonate (ANS) bound to egg lecithin liposomes and also to increase the maximum fluorescence value, as derived from double reciprocal plots. The assay conditions were such that addition of valinomycin would not produce a transmembrane potential. The formation of a valinomycin potassium ANS complex in the micelle membrane is proposed. This could account for the increase in the maximum fluorescence value and, by acting as an ANS transporter, could also account for the increase in ANS bound. Tributylamine was also shown to increase the binding and maximum fluorescence of ANS. In assay conditions where the addition of valinomycin would produce a transmembrane potential negative inside, the tributylamine-induced fluorescence was reversed. The fluorescense decrease is interpreted as transmembrane electrophoresis of ANS in response to a transmembrane potential.
D000817:Anilino Naphthalenesulfonates / Q000378:metabolism*; D001665:Binding Sites; D002082:Butylamines / Q000494:pharmacology; D008081:Liposomes / Q000378:metabolism*; D008567:Membranes, Artificial; D010539:Permeability; D010713:Phosphatidylcholines; D011189:Potassium Chloride / Q000494:pharmacology; D013010:Sonication; D014634:Valinomycin / Q000494:pharmacology
D000817:Anilino Naphthalenesulfonates; D002082:Butylamines; D008081:Liposomes; D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D014634:Valinomycin; D011189:Potassium Chloride