gamma-Aminobutyric acid and benzodiazepine receptors: copurification and characterization.
AUTOR(ES)
Gavish, M
RESUMO
gamma-Aminobutyric acid (GABA) and benzodiazepine receptors have been solubilized and purified by procedures such as gel filtration, ion-exchange, lectin, and affinity chromatographies. 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 association of GABA, benzodiazepine, and chloride recognition sites after extensive purification suggests that they may be part of a single macromolecular complex.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=319251Documentos Relacionados
- Stimulation of benzodiazepine receptor binding by gamma-aminobutyric acid.
- Monoclonal antibodies reveal structural homogeneity of gamma-aminobutyric acid/benzodiazepine receptors in different brain areas.
- Benzodiazepine-insensitive mice generated by targeted disruption of the gamma 2 subunit gene of gamma-aminobutyric acid type A receptors.
- Autoradiographic localization of gamma-aminobutyric acid (GABA) receptors in the rat cerebellum.
- Stable expression of mammalian type A gamma-aminobutyric acid receptors in mouse cells: demonstration of functional assembly of benzodiazepine-responsive sites.
