title: Ligand binding specificity of a neutral L-amino acid olfactory receptor.
abstract: 1. The ligand binding specificity of the L-[3H]alanine binding site was investigated in isolated cilia preparations from the olfactory epithelium of channel catfish (Ictalurus punctatus) by competitive binding experiments. 2. Approximately 45 amino acids, derivatives and enantiomers were tested for the ability to compete with radiolabeled L-alanine for common binding sites. 3. Acidic and basic L-amino acids and imino acids did not compete as effectively as L-alanine for the receptor, while long-chain neutral ligands were only partially effective inhibitors of L-alanine binding. 4. D-Alanine and L-alanine derivatives with substituted alpha-amino or carboxyl groups exhibited decreased ability to compete for the receptor, paralleling their lower neurophysiological potency. 5. In combination, the ligand binding results were consistent with previous electrophysiological data in catfish, and suggest the presence of an olfactory receptor site that selectively recognizes short-chain neutral amino acids.
authors.affiliation: Monell Chemical Senses Center, Philadelphia, PA 19104.
authors.forename: R C
authors.initials: RC
authors.lastname: Bruch
authors.forename: R D
authors.initials: RD
authors.lastname: Rulli
mesh_terms: D000409:Alanine / Q000378:metabolism; D000818:Animals; D001667:Binding, Competitive; D007059:Ictaluridae / Q000378:metabolism; D009831:Olfactory Mucosa / Q000378:metabolism*; D017459:Receptors, Amino Acid; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013237:Stereoisomerism
chemical_list: D017459:Receptors, Amino Acid; D011956:Receptors, Cell Surface; D000409:Alanine