GABA receptor binding in bovine retina: Effects of triton X-100 and perchloric acid

Abstract

In two synaptosomal fractions from bovine retina, Triton X-100 and sodium perchlorate specifically enhanced the high affinity binding of 3H-GABA to sites with pharmacological specificity similar to the GABA receptor. Maximal effects were noted at 0.05% Triton X-100 and 100 mM sodium perchlorate. In the fraction enriched in photoreceptor cell synaptosomes from the outer plexiform layer, Triton and perchlorate had similar effects in that two binding sites were observed: a higher affinity site (∼20 nMK D) and a lower affinity site (∼200 nMK D). However, in the fraction enriched in conventional sized synaptosomes primarily from the inner plexiform layer, the 20 nM site was virtually absent after Triton treatment, but was readily detectable in the presence of perchlorate. These results may suggest that 3H-GABA binding in vitro is inhibited by an endogenous substance which is removed by Triton or perchlorate treatment. The difference in the sensitivity of the two fractions to Triton and perchlorate suggests that in retina this substance (whether it is a membrane peptide or GABA itself) is not uniformly distributed and/or uniformly sensitive to Triton and perchlorate.