Separation of alpha 1, alpha 2 and alpha 3 subunits of the GABAA-benzodiazepine receptor complex by immunoaffinity chromatography.
Polyclonal antibodies raised to synthetic amino acid sequences of the rat gamma-aminobutyric acid (GABAA) receptor alpha 1-, alpha 2- and alpha 3-subunits selectively recognized single proteins with apparent molecular weight 51 kDa (P51), 53 kDa (P53) and 59 kDa (P59), respectively, in GABAA receptor preparations affinity purified from the brains of 5-10-day-old rats. The antibodies were coupled to Affigel 10, and the resulting immunoaffinity columns were used to isolate these proteins from affinity purified GABAA receptors.
Zezula
J
J
Department of Biochemical Psychiatry, Universitätsklinik für Psychiatrie, Vienna, Austria.
Fuchs
K
K
Sieghart
W
W
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002846:Chromatography, Affinity; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D051381:Rats; D011963:Receptors, GABA-A / Q000737:chemistry* / Q000276:immunology
D010455:Peptides; D011963:Receptors, GABA-A