Citation

Cousin X, Créminon C, Grassi J, Méflah K, Cornu G, Saliou B, Bon S, Massoulié J, Bon C. FEBS Lett. 1996; 387(2-3): 196-200.

Affiliation

Unité des Venins, Institut Pasteur, Paris, France.

Copyright

(Copyright © 1996, Federation of European Biochemical Societies, Publisher Elsevier Publishing)

DOI

unavailable

PMID

8674549

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.

Language: en