Abstract
Cilia isolated fromParamecium tetraurelia possess a specific, high affinity L-[3H]glutamic acid binding site, defined by an ED50 of 3.0×10−8 M. The structural specificity of this site was probed by testing the competition between L-glutamate and various analogues for binding to cilia. The binding site is stereo-specific for L-glutamic acid, and requires the presence of all three ionizable groups on the glutamate molecule for optimal ligand: receptor interaction. Specific binding of L-[3H]glutamic acid to cilia is rapid in onset but transient, reaching peak values within 6 min, and then declining thereafter. This transience may represent a form of sensory adaptation during prolonged exposure to the ligand.
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