Quantitative Characterization of α6 and α1α6 Subunit-containing Native γ-Aminobutyric AcidA Receptors of Adult Rat Cerebellum Demonstrates Two α Subunits per Receptor Oligomer

作者: Simon Pollard , Christopher L. Thompson , F. Anne Stephenson

DOI: 10.1074/JBC.270.36.21285

关键词: CopurificationGABAA receptorBiochemistryMolecular biologyProtein subunitPopulationInterleukin 10 receptor, alpha subunitReceptorInterleukin 5 receptor alpha subunitBiologyCys-loop receptors

摘要: γ-Aminobutyric acidA (GABAA) receptors were purified from adult rat cerebella by anti-α6(1-16 Cys) antibody affinity chromatography. Immunoblots of the α6 subunit-containing showed copurification α1, β2/3, γ2, δ but not α2 and α3 GABAA receptor polypeptides. Further fractionation this subpopulation anti-GABAA subunit α6(1-16 anti-α1(413-429) columns in series substantiated coassociation α1 The percentage coexistence two subunits was determined quantitative immunoblotting, which found that 41 ± 12% immunoreactivity is associated with subunit. ratios α1:α6 double preparations to be 1:1, thus determining directly for first time within native receptors. benzodiazepine pharmacology α1α6 shown predominantly benzodiazepine-insensitive immunoprecipitation assays. These results are direct studies a population

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