Abstract
Abstract: Binding of [3H]taurine to whole retinal membranes and to membranes obtained from retinal subcellular fractions was studied. [3H]Taurine bound to chick retinal membranes with high affinity and specificity. Two types of [3H]taurine binding associated to retinal membranes were observed, one with a KD= 0.68 μM and the other one with a KD,= 9.32 μM. Both types of binding were highly Na−‐dependent. The Na+‐dependent taurine binding was antagonized by strychnine. Bound [3H]taurine was effectively displaced by β‐alanine but not by GABA or glycine. Taurine binding was preferentially localized in membranes obtained from the crude synaptosomal fraction, although it is also present in substantial amounts in all retinal membranes. A Na+‐independent [3H]taurine binding exhibiting properties which might represent interaction with postsynaptic receptor sites could not be demonstrated in the chick retina.
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