The monensin-mediated transport of Na+ and K+ through phospholipid bilayers studied by 23Na- and 39K-NMR

Biochim Biophys Acta. 1988 Oct 6;944(2):279-84. doi: 10.1016/0005-2736(88)90442-7.


Addition of monesin to preparations of large unilamellar vesicles made from egg yolk phosphatidylcholine (EPC) in sodium or potassium chloride solution and from dioleoylphosphatidylcholine (DOPC) in sodium chloride solutions gives rise to dynamic 23Na- and 39K-NMR spectra. The dynamic spectra arise from the monensin-mediated transport of the metal ions through the membrane. The kinetics of the transport are followed as a function of monensin and metal ion concentrations and are compatible with a model in which one monensin molecule transports one metal ion. Rate constants for the association and dissociation of the monensin-metal complex in the membrane/water interface are extracted and the stability constants for complex formation are evaluated. The rate constants in DOPC are similar to those in EPC, confirming that diffusion is not rate-limiting in the transport process and that dissociation of the complex is the rate-limiting step. Although potassium on its own is transported more rapidly, sodium forms the more stable complex and is therefore transported preferentially in competition with potassium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport, Active
  • Lipid Bilayers / metabolism*
  • Magnetic Resonance Spectroscopy
  • Monensin / pharmacology*
  • Phospholipids
  • Potassium / pharmacokinetics*
  • Potassium Isotopes
  • Sodium / pharmacokinetics*
  • Sodium Isotopes


  • Lipid Bilayers
  • Phospholipids
  • Potassium Isotopes
  • Sodium Isotopes
  • Monensin
  • Sodium
  • Potassium