Acetylcholinesterase from Bungarus venom: a monomeric species.
(1996) FEBS Letters — Vol. 387, n° 2-3, p. 196-200 (1996)
Files
pdfdocument.pdf
Restricted Access - Adobe PDF
- 546.94 KB
Details
- Authors
- 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.
- Affiliations
Citations
Cousin, X., Créminon, C., Grassi, J., Méflah, K., Cornu, G., Saliou, B., Bon, S., Massoulié, J., & Bon, C. (1996). Acetylcholinesterase from Bungarus venom: a monomeric species. FEBS Letters, 387(2-3), 196-200. https://doi.org/10.1016/0014-5793(96)00447-4 (Original work published 1996)