Learn More
The action of gramicidin S and melittin on human erythrocytes, Staphylococcus aureus and Escherichia coli was studied as an extension of the previous study (Katsu, T., Ninomiya, C., Kuroko, M., Kobayashi, H., Hirota, T. and Fujita, Y. (1988) Biochim. Biophys. Acta 939, 57-63). These amphipathic peptides stimulated the release of membrane phospholipids(More)
Mastoparan-induced changes in the K+ permeability of rat peritoneal mast cells, human erythrocytes, Staphylococcus aureus and Escherichia coli were examined. Mastoparan did not efficiently increase the K+ permeability of cells except for S. aureus. The release of membrane phospholipids was also observed from S. aureus cells in the concentration range of the(More)
The gramicidin S analog lacking basic ornithine residues, cyclo(-Val-Ala-Leu-delta Phe-Pro-)2 (where delta Phe represents alpha, beta-dehydrophenylalanine), increased the K+ permeability of human erythrocytes and Staphylococcus aureus similarly to the parent gramicidin S. This analog altered the normal discoid shape of human erythrocytes to an invaginated(More)
Amphiphile-induced tetraethylammonium ion (TEA+) uptake into human erythrocytes was examined along with cell shape change. A TEA(+)-sensitive electrode was used to determine the amount of uptake. TEA+ was preferentially incorporated into erythrocytes when amphiphiles changed cell shape to an invaginated form. This was contrasted with the release of(More)
  • 1