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Effect of Halide Ions on t-[³⁵S]Butylbicyclophosphorothionate Binding

Kennon M. Garrett

Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, Lederle Laboratories, Pearl River, New York, U.S.A.

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Arthur J. Blume,

Arthur J. Blume

Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, Lederle Laboratories, Pearl River, New York, U.S.A.

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Marc S. Abel,

Corresponding Author

Marc S. Abel

Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, Lederle Laboratories, Pearl River, New York, U.S.A.

Address correspondence and reprint requests to Dr. M. S. Abel at Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, 56B/137, Lederle Laboratories, Pearl River, NY 10965, U.S.A.Search for more papers by this author

Kennon M. Garrett,

Kennon M. Garrett

Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, Lederle Laboratories, Pearl River, New York, U.S.A.

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Arthur J. Blume,

Arthur J. Blume

Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, Lederle Laboratories, Pearl River, New York, U.S.A.

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Marc S. Abel,

Corresponding Author

Marc S. Abel

Molecular Neurobiology, Department of Central Nervous System Research, Medical Research Division of American Cyanamid Company, Lederle Laboratories, Pearl River, New York, U.S.A.

First published: September 1989

https://doi.org/10.1111/j.1471-4159.1989.tb11795.x

Citations: 4

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Abstract

The binding of t-[³⁵S]butylbicyclophosphoro-thionate ([³⁵S]TBPS) to a site on the GABA_A receptor complex is ion dependent. This study was conducted to determine the effects of ion species and concentration on the time course, affinity, and number of sites of [³⁵S]TBPS binding. At a concentration of 200 mM ion, the time to equilibrium for [³⁵S]TBPS binding was shortest for I^-, followed by Br^-< CI^-< F^-. A similar rank order was observed for the concentration of ion required to produce half-maximal [³⁵S]TBPS binding. Saturation binding experiments were conducted to evaluate the effect of increasing ion concentration on the K_D and B_max of [³⁵S]TBPS binding. The B_max was independent of both ion species and concentration. The receptor affinity, however, increased with increasing concentration for each ion. Calculated maximal affinity values were not different between ions; however, the EC₅₀ to produce those values was different among ions and ranked in the same order as that for time course and maximal binding data. Association and dissociation rates for [³⁵S]TBPS binding were greater in I^- than in Cl^-. These data emphasize the importance of ion selection and incubation times on [³⁵S]TBPS binding.

Abbreviations used:

GABA: γ-aminobutyric acid
TBPS: t-butyl-bicyclophosphorothionate

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Volume53, Issue3

September 1989

Pages 935-939

Effect of Halide Ions on t-[³⁵S]Butylbicyclophosphorothionate Binding

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Effect of Halide Ions on t-[³⁵S]Butylbicyclophosphorothionate Binding