Acetylcholinesterase from Drosophila melanogaster Identification of two subunits encoded by the same gene

FEBS Letters

Karch, François²  Bride, Jean-Marc¹  Fournier, Didier¹  Bergé, Jean-Baptiste¹ 

[1] INRA, Centre de Recherche d'Antibes, BP 2078, 06600 Antibes, France;Université de Genève, Dépt. de Biologie Animale, 154 bis route de Malagnou, 1224 Chêne-Bougeries, Genève, Switzerland

关键词: Acetylcholinesterase;    Polypeptide;    (Drosophila);    AChE;    acetylcholinesterase;    BuChE;    butyrylcholinesterase;    DFP;    diisopropyl fluorophosphate;   

DOI  :  10.1016/0014-5793(88)80507-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Purified acetylcholinesterase from Drosophila melanogaster is composed of a 55 kDa and a 16 kDa noncovalently associated subunit. Cleavage of disulfide bonds reveals that two 55 kDa polypeptides are linked together in native dimeric AChE. Western blots with two antibodies directed against the N- and C-termini of the predicted AChE primary sequence show that the 55 and 16 kDa polypeptides originate from proteolysis of the same precursor encoded by the Ace locus.

【 授权许可】

Unknown