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Acetylcholinesterase from Bungarus venom: a monomeric species
Author(s) -
Cousin Xavier,
Crémi Christophe,
Grassi Jacques,
Méflah Khaled,
Cornu Gur,
Saliou Bernard,
Bon Suzanne,
Massoulié Jean,
Bon Cassian
Publication year - 1996
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(96)00447-4
Subject(s) - venom , acetylcholinesterase , elapidae , isoelectric focusing , biochemistry , chemistry , glycan , isoelectric point , monomer , glycosylation , enzyme , amphiphile , gel electrophoresis , glycoprotein , organic chemistry , polymer , copolymer
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.