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Identification of α 2 ‐ and α 3 ‐subunits of the GABA A ‐benzodiazepine receptor complex purified from the brains of young rats
Author(s) -
Fuchs K.,
Adamiker D.,
Sieghart W.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80634-u
Subject(s) - flunitrazepam , polyclonal antibodies , receptor , monoclonal antibody , peptide , microbiology and biotechnology , immunoprecipitation , antibody , protein subunit , chemistry , gabaa receptor , affinity chromatography , blot , biochemistry , benzodiazepine , biology , enzyme , immunology , gene
Polyclonal antibodies were raised to synthetic amino acid sequences of the bovine GABA A receptor α 2 ‐ and α 3 ‐subunits and purified by affinity chromatography on a column coupled with the respective peptide. Anti‐peptide α 2 (416–424) and anti‐peptide α 3 (459–467) antibodies immunoprecipitated GABA A receptors and recognized a protein of 53 kDa (P 53 ) and 59 kDa (P 59 ), respectively, in Western blots of GABA A receptors purified from the brains of 5–10 day old rats. P 53 as well as P 59 are specifically photolabeled by [ 3 H]flunitrazepam and are recognized by the α‐subunit specific monoclonal antibody bd 28.