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Acetylcholinesterase from Drosophila melanogaster Identification of two subunits encoded by the same gene
Author(s) -
Fournier Didier,
Bride Jean-Marc,
Karch François,
Bergé Jean-Baptiste
Publication year - 1988
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(88)80507-6
Subject(s) - drosophila melanogaster , acetylcholinesterase , proteolysis , protein subunit , gene , locus (genetics) , disulfide bond , biochemistry , microbiology and biotechnology , cleavage (geology) , protein primary structure , chemistry , biology , enzyme , peptide sequence , paleontology , fracture (geology)
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.