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Enhancement of t ‐[ 35 S]Butylbicyclophosphorothionate and [ 3 H]Strychnine Binding by Monovalent Anions Reveals Similarities Between γ‐Aminobutyric Acid‐ and Glycine‐Gated Chloride Channels
Author(s) -
Marvizón Juan Carlos G.,
Skolnick Phil
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb03053.x
Subject(s) - strychnine , glycine , aminobutyric acid , chloride channel , chemistry , chloride , glycine receptor , biophysics , amino acid , biochemistry , biology , organic chemistry , receptor
The characteristics of [ 3 H]strychnine and t ‐[ 35 S]‐butylbicyclophosphorothionate ([ 35 S]TBPS) binding to sites associated with glycine‐ and γ‐aminobutyric acid (GABA)‐gated chloride channels were compared in the presence of a series of anions with known permeabilities through these channels. Good correlations were found between (a) the potencies (EC 50 ) of these anions to stimulate radioligand binding and their permeabilities relative to chloride; (b) the affinities ( K D ) of these radioligands in the presence of fixed concentrations of these anions and their relative permeabilities; (c) the potencies (EC 50 ) of these anions to stimulate [ 35 S]TBPS and [ 3 H]strychnine binding; and (d) the affinities ( K D ) of [ 3 H]strychnine and [ 35 S]TBPS measured at a fixed concentration of these anions. These studies support electrophysiological and biochemical observations demonstrating similarities between glycine‐ and GABA‐gated chloride channels, and suggest that anions enhance [ 3 H]strychnine and [ 35 S]TBPS binding through specific anion binding sites located at the channels.