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Neuronal nicotinic acetylcholine receptor β‐subunit is coded for by the cDNA clone α4

机译:神经元烟碱型乙酰胆碱受体β亚基由cDNA克隆α4编码

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>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 α3 and α4 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 α4. Further, we present evidence consistent with a subunit stoichiometry of α3β2 for this neuronal nicotinic AChR.
机译:>通过免疫亲和层析从大鼠和鸡脑中纯化出的对尼古丁具有高亲和力但对α-真菌毒素无亲和力的乙酰胆碱受体(AChR)由两种亚基,α和β组成[1,2 ]。 β亚基形成ACh结合位点[3]。通过用编码小鼠肌肉AChRα亚基的cDNA探针筛选从大鼠PC12细胞和大鼠脑制备的cDNA文库,鉴定出了假定的烟碱AChR亚基cDNAα 3 和α 4 。在这里,我们通过蛋白质微测序确定大鼠脑AChRβ亚基的氨基末端氨基酸序列与该蛋白质的氨基酸残基27–43相同,可以由α 4 编码。此外,我们目前提供的证据与该神经元烟碱型AChR的亚基化学计量比α 3 β 2 一致。

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