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Neuronal nicotinic acetylcholine receptor β‐subunit is coded for by the cDNA clone α 4
Author(s) -
Whiting Paul,
Esch Fred,
Shimasaki S.,
Lindstrom Jon
Publication year - 1987
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(87)80272-7
Subject(s) - acetylcholine receptor , protein subunit , nicotinic acetylcholine receptor , complementary dna , nicotinic agonist , amino acid , microbiology and biotechnology , biochemistry , cys loop receptors , biology , peptide sequence , gamma aminobutyric acid receptor subunit alpha 1 , alpha 4 beta 2 nicotinic receptor , acetylcholine , affinity chromatography , receptor , g alpha subunit , enzyme , endocrinology , gene
Acetylcholine receptors (AChRs) with high affinity for nicotine but no affinity for α‐bungarotoxin, which have been purified from rat and chicken brains by immuno‐affinity chromatography, consist of two types of subunits, α and β [1,2]. The β‐subunits form the ACh binding sites [3]. Putative nicotinic AChR subunit cDNAs α 3 and α 4 have been identified by screening cDNA libraries prepared from rat PC12 cells and rat brain with cDNA probes encoding the mouse muscle AChR α‐subunit. Here we determine the amino‐terminal amino acid sequence of the rat brain AChR β‐subunit by protein microsequencing to be the same as amino acid residues 27–43 of the protein which could be coded by α 4 . Further, we present evidence consistent with a subunit stoichiometry of α 3 β 2 for this neuronal nicotinic AChR.