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BINDING OF [ 3 H]‐MUSCIMOL, A POTENT γ‐AMINOBUTYRIC ACID RECEPTOR AGONIST, TO MEMBRANES OF THE BOVINE RETINA
Author(s) -
OSBORNE NEVILLE N.
Publication year - 1980
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1980.tb10934.x
Subject(s) - muscimol , agonist , aminobutyric acid , chemistry , binding site , gabaa receptor , membrane , receptor , sodium , biochemistry , biophysics , biology , organic chemistry
1 The binding of [ 3 H]‐muscimol, a potent γ‐aminobutyric acid (GABA) receptor agonist, to crude membrane preparations of bovine retina was studied, using a filtration method to isolate membranebound ligand. 2 Specific binding was found to be saturable and occurred at two binding sites with affinity constants of 4.3 n m and 38.2 n m . 3 Binding was sodium‐independent, enhanced by both freezing and Triton X‐100 treatment but abolished with sodium laurylsulphate. 4 The binding sites demonstrated a high degree of pharmacological specificity, GABA being a potent displacer of [ 3 H]‐muscimol. 5 A higher degree of [ 3 H]‐muscimol binding was associated with subcellular fractions enriched with photoreceptor synaptosomes rather than with fractions enriched with conventional synaptosomes.

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