Acetylcholinesterase from Drosophila melanogaster. Identification of two subunits encoded by the same gene.
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.
D000110:Acetylcholinesterase / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000235:genetics; D004220:Disulfides / Q000378:metabolism; D004331:Drosophila melanogaster / Q000201:enzymology* / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D007118:Immunoassay; D007531:Isoflurophate / Q000378:metabolism; D046911:Macromolecular Substances; D008969:Molecular Sequence Data
D004220:Disulfides; D046911:Macromolecular Substances; D007531:Isoflurophate; D004247:DNA; D000110:Acetylcholinesterase