Plümer R, Fels G, Maelicke A
FEBS Lett. 1984 Dec 10;178(2):204-8. doi: 10.1016/0014-5793(84)80601-8.
Rabbit immune sera and mouse monoclonal antibodies were raised against the synthetic peptide Tyr-Cys-Glu-Ile-Ile-Val matching in sequence residues 127-132 of the alpha-subunit of all nicotinic acetylcholine receptors sequenced so far. Representative cholinergic ligands did not interfere with the binding of these antibodies to the receptor from Torpedo marmorata, indicating that this sequence is not part of the binding sites for cholinergic ligands. The applicability of antigenic sites analysis to the mapping of functional sites on receptor proteins is discussed.
针对合成肽Tyr-Cys-Glu-Ile-Ile-Val制备了兔免疫血清和小鼠单克隆抗体,该肽与迄今测序的所有烟碱型乙酰胆碱受体α亚基的127 - 132位序列残基相匹配。典型的胆碱能配体并不干扰这些抗体与电鳐受体的结合,这表明该序列不是胆碱能配体结合位点的一部分。本文讨论了抗原位点分析在受体蛋白功能位点图谱绘制中的适用性。