Cousin_1996_FEBS.Lett_387_196

Reference

Title : Acetylcholinesterase from Bungarus venom: a monomeric species - Cousin_1996_FEBS.Lett_387_196
Author(s) : Cousin X , Creminon C , Grassi J , Meflah K , Cornu G , Saliou B , Bon S , Massoulie J , Bon C
Ref : FEBS Letters , 387 :196 , 1996
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.

PubMedSearch : Cousin_1996_FEBS.Lett_387_196
PubMedID: 8674549

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Citations formats

Cousin X, Creminon C, Grassi J, Meflah K, Cornu G, Saliou B, Bon S, Massoulie J, Bon C (1996)
Acetylcholinesterase from Bungarus venom: a monomeric species
FEBS Letters 387 :196

Cousin X, Creminon C, Grassi J, Meflah K, Cornu G, Saliou B, Bon S, Massoulie J, Bon C (1996)
FEBS Letters 387 :196