-
Acetylcholinesterase from Drosophila melanogaster. Identification of two subunits encoded by the same gene.
INRA, Centre de Recherche d'Antibes, France.
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.
PMID: 3139459 [PubMed - indexed for MEDLINE]
-
Cited by 2 PubMed Central articles
-
ReviewRelationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.
Cygler M, Schrag JD, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP.
Protein Sci. 1993 Mar; 2(3):366-82.
[Protein Sci. 1993]
-
Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid.
Krejci E, Duval N, Chatonnet A, Vincens P, Massoulié J.
Proc Natl Acad Sci U S A. 1991 Aug 1; 88(15):6647-51.
[Proc Natl Acad Sci U S A. 1991]