Properties of gramicidin A channels in erythrocyte membranes.
Studies for the cation permeability properties of the gramicidin A channel in erythrocyte membranes are presented. It is shown that gramicidin A interacts with the membrane in a cooperative manner, creating aggregates of the antibiotic molecules in the lipid lattice of the membrane. Cationic channels exist in these aggregates with the following order of selectivity: Rb+ greater than Cs+ greater K+ greater than Na+. The cation permeability of the channels depends on the media surrounding the membrane. This finding has been explained on the basis of Hodgkin-Keynes theory for single-file ion diffusion through extra-narrow pores.
Blaskó
K
K
Institute of Biophysics, Semmelweis Medical University, Budapest, Hungary.
Schagina
L V
LV
Györgyi
S
S
Rontó
G
G
D002412:Cations; D002463:Cell Membrane Permeability; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006096:Gramicidin / Q000378:metabolism*; D007473:Ion Channels; D011197:Potassium Radioisotopes; D012414:Rubidium Radioisotopes; D012979:Sodium Radioisotopes
D002412:Cations; D007473:Ion Channels; D011197:Potassium Radioisotopes; D012414:Rubidium Radioisotopes; D012979:Sodium Radioisotopes; D006096:Gramicidin