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Acetylcholinesterase from Bungarus venom: a monomeric species.

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Cousin, X Créminon, C Grassi, J. Méflah, K Cornu, Guy [UCL] Bon, C

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.

Document type Article de périodique (Journal article) – Journal Article
Access type Accès restreint
Publication date 1996
Journal information "FEBS letters" - Vol. 387, no. 2-3, p. 196-200 (1996)
Peer reviewed yes
issn 0014-5793
Publication status Publié
Affiliation UCL
MESH Subject Acetylcholinesterase - analysis - chemistry - toxicity ; Amino Acid Sequence ; Animals ; Bungarotoxins - chemistry - toxicity ; Bungarus ; Carbohydrates - analysis ; Electrochemistry ; Male ; Mice ; Molecular Sequence Data ; Sequence Homology, Amino Acid
Links
  1. Massoulié Jean, Pezzementi Leo, Bon Suzanne, Krejci Eric, Vallette François-Marie, Molecular and cellular biology of cholinesterases, 10.1016/0301-0082(93)90040-y
  2. Toutant J.-P., Massoulié J., Cholinesterases: Tissue and Cellular Distribution of Molecular Forms and Their Physiological Regulation, The Cholinergic Synapse (1988) ISBN:9783642732225 p.225-265, 10.1007/978-3-642-73220-1_9
  3. Kumar Vijay, Elliott Willard Buford, The Acetylcholinesterase of Bungarus fasciatus Venom, 10.1111/j.1432-1033.1973.tb02799.x
  4. Kreienkamp, Proc. Natl. Acad. Sci. USA, 88, 6117 (1991)
  5. Weise Christoph, Kreienkamp Hans-J�rgen, Raba Raivo, Aaviksaar Aavo, Hucho Ferdinand, The active site and partial sequence of cobra venom acetylcholinesterase, 10.1007/bf01024984
  6. Ellman George L., Courtney K.Diane, Andres Valentino, Featherstone Robert M., A new and rapid colorimetric determination of acetylcholinesterase activity, 10.1016/0006-2952(61)90145-9
  7. MASSOULIE Jean, BON Suzanne, Affinity Chromatography of Acetylcholinesterase. The Importance of Hydrophobic Interactions, 10.1111/j.1432-1033.1976.tb10841.x
  8. Duval N., H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms, 10.1083/jcb.118.3.641
  9. KARNOVSKY MORRIS J., ROOTS LOGAN, A "DIRECT-COLORING" THIOCHOLINE METHOD FOR CHOLINESTERASES, 10.1177/12.3.219
  10. Pan, Prog. Drug Res., 34, 162 (1990)
  11. Cousin, J. Biol. Chem. (1996)
  12. Porschke D., Créminon C., Cousin X., Bon C., Sussman J., Silman I., Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase, 10.1016/s0006-3495(96)79759-x
  13. RABA Raivo, AAVIKSAAR Aavo, RABA Mari, SIIGUR Juri, Cobra Venom Acetylcholinesterase. Purification and Molecular Properties, 10.1111/j.1432-1033.1979.tb13024.x
  14. Bon Suzanne, Rosenberry Terrone L., Massouli� Jean, Amphiphilic, glycophosphatidylinositol-specific phospholipase C (PI-PLC)-insensitive monomers and dimers of acetylcholinesterase, 10.1007/bf00712807
  15. RABA Raivo, AAVIKSAAR Aavo, Cobra Venom Acetylcholinesterase: Nature of Charge Isoforms, 10.1111/j.1432-1033.1982.tb06900.x
  16. YANG CHEN-CHUNG, KAO KUANG-CHING, CHIU WEN-CHING, BIOCHEMICAL STUDIES ON THE SNAKE VENOMS, 10.1093/oxfordjournals.jbchem.a127222
  17. Chang, Arch. Int. Pharmacodyn., 144, 241 (1963)
Bibliographic reference Cousin, X ; Créminon, C ; Grassi, J. ; Méflah, K ; Cornu, Guy ; et. al. Acetylcholinesterase from Bungarus venom: a monomeric species.. In: FEBS letters, Vol. 387, no. 2-3, p. 196-200 (1996)
Permanent URL http://hdl.handle.net/2078.1/27190