The mechanism of potassium movement across the liposomal membrane.

Addition of potassium to sodium-loaded asolectin liposomes induces an internal alkalinization even in the absence of ionophores. Most of the K+ entry is electrogenic, as shown by fluorescent changes in the potential-sensitive probe Oxonol V. The major part of the proton efflux observed must therefore be electrophoretic. However, in the presence of high concentrations of membrane permeable n-butyltriphenylphosphonium, potassium addition induces a residual alkalinization under conditions where no membrane potential can be observed with Oxonol V. This suggests that liposomes also catalyze direct electroneutral K+/H+ exchange, as has been theoretically predicted for cytochrome oxidase proteoliposomes (Wrigglesworth, J.M., Cooper, C.E., Sharpe, M.A. and Nicholls, P. (1990) Biochem. J. 270, 109-118). Free fatty acids present in the soybean phospholipid mixture may be responsible for such activity.