title: Acetylcholinesterase from Bungarus venom: a monomeric species.
abstract: The venom of Bungarus fasciatus, an Elapidae snake, contains a high level of AChE activity. Partial peptide sequences show that it is closely homologous to other AChEs. Bungarus venom AChE is a non-amphiphilic monomeric species, a molecular form of AChE which has not been previously found in significant levels in other tissues. The composition of carbohydrates suggests the presence of N-glycans of the 'complex' and 'hybrid' types. Ion exchange chromatography, isoelectric focusing and electrophoresis in non-denaturing and denaturing conditions reveal a complex microheterogeneity of this enzyme, which is partly related to its glycosylation.
authors.affiliation: Unité des Venins, Institut Pasteur, Paris, France.
authors.forename: X
authors.initials: X
authors.lastname: Cousin
authors.forename: C
authors.initials: C
authors.lastname: Créminon
authors.forename: J
authors.initials: J
authors.lastname: Grassi
authors.forename: K
authors.initials: K
authors.lastname: Méflah
authors.forename: G
authors.initials: G
authors.lastname: Cornu
authors.forename: B
authors.initials: B
authors.lastname: Saliou
authors.forename: S
authors.initials: S
authors.lastname: Bon
authors.forename: J
authors.initials: J
authors.lastname: Massoulié
authors.forename: C
authors.initials: C
authors.lastname: Bon
mesh_terms: D000110:Acetylcholinesterase / Q000032:analysis* / Q000737:chemistry / Q000633:toxicity; D000595:Amino Acid Sequence; D000818:Animals; D002038:Bungarotoxins / Q000737:chemistry* / Q000633:toxicity; D017838:Bungarus; D002241:Carbohydrates / Q000032:analysis; D004563:Electrochemistry; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
chemical_list: D002038:Bungarotoxins; D002241:Carbohydrates; D000110:Acetylcholinesterase