γ-Aminobutyric acid and benzodiazepine receptors: Copurification and characterization

M. Gavish, Solomon H Snyder

Research output: Contribution to journalArticle

Abstract

γ-Aminobutyric acid (GABA) and benzodiazepine receptors have been solubilized and purified by procedures such as gel filtration, ion-exchange, lectin, and affinity chrmatographies. All of these procedures enhance the specific activity of each receptor to a similar extent. The drug specificities of [3H]muscimol and [3H]flunitrazepam binding sites are the same after extensive purification by affinity chromatography compared to the membrane bound and initially solubilized receptors. GABA and chloride stimulation of benzodiazepine binding is retained in pure receptors. Two bands are covalently labeled with [3H]flunitrazepam after ultraviolet irradiation of the purified receptor. The persistent assocition of GABA, benzodiazepine, and chloride recognition sites after extensive purification suggests that they may be part of a single macromolecular complex.

Original languageEnglish (US)
Pages (from-to)1939-1942
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number3 I
StatePublished - 1981

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Aminobutyrates
Flunitrazepam
GABA-A Receptors
Benzodiazepines
gamma-Aminobutyric Acid
Chlorides
Macromolecular Substances
Muscimol
Ion Exchange
Affinity Chromatography
Lectins
Gel Chromatography
Binding Sites
Membranes
Pharmaceutical Preparations

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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