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The inside-out configuration of the patch-clamp technique was used to study the effects of large organic cations on the single-channel current through the glutamate receptor channel in muscles of Drosophila larvae. Control experiments with symmetrical Na+ showed slightly supra-linear I-V curves. When external Na+ was equiosmolarly replaced with either arginine+ or N-methyl-D-glucamine+ (NMDG+), the reversal potential changed almost according to VNa, suggesting that both these ions are only slightly permeant through the channel. However, both ions strongly reduced the current amplitude in a voltage-dependent manner, the effect being most pronounced for the inward current. Tris+ had similar effects on the Na+ current, although the reversal potential indicated that this ion is somewhat permeant. All of these results could be fitted with a "one-ion" Eyring model for the channel with internal binding sites. The ion-channel dissociation constants for arginine+, NMDG+, and Tris+ were found to be 17, 27, and 23 mM, respectively. In order to acquire evidence for the "one-ion" hypothesis used in the model, I-V data were taken with different mixtures of Na+ and a comparably permeant ion, NH4+. All of the data could be accurately fitted with the results of the Eyring theory for singly occupied channels.

Permeation of Organic Cations and Ammonium through the Glutamate Receptor Channel in Drosophila Larval Muscle.