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N ‐Deglycosylation and immunological identification indicates the existence of β‐subunit isoforms of the rat GABA A receptor
Author(s) -
Buchstaller A.,
Adamiker D.,
Fuchs K.,
Sieghart W.
Publication year - 1991
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(91)80008-q
Subject(s) - polyclonal antibodies , gene isoform , protein subunit , receptor , monoclonal antibody , alternative splicing , gamma aminobutyric acid receptor subunit alpha 1 , biochemistry , interleukin 10 receptor, alpha subunit , microbiology and biotechnology , chemistry , interleukin 12 receptor, beta 1 subunit , antibody , biology , g alpha subunit , genetics , gene
β 2 ‐ and β 3 ‐subunits of GABA A receptors purified from the brains of 5–10‐day‐old rats were investigated in the intact or completely N ‐deglycosylated state using the β‐subunit‐specific monoclonal antibody bd‐17 and polyclonal antibodies directed against synthetic amino acid sequences specific for the GABA A receptor β 2 ‐ or β 3 ‐subunits. The present results seem to indicate the existence of two different isoforms of the β 3 ‐subunit and several different isoforms of the β 2 ‐subunit of the GABA A receptor which probably are produced by alternative splicing.