Acetylcholinesterase from Bungarus venom: a monomeric species

FEBS Letters

Massoulié, Jean²  Grassi, Jacques⁴  Méflah, Khaled¹  Bon, Suzanne²  Cornu, Gur¹  Créminon, Christophe⁴  Bon, Cassian³  Saliou, Bernard³  Cousin, Xavier³ 

[1] Unité INSERM 419, 9 Quai Moncousu, 44035, Nantes cedex 01, France;Laboratoire de Neurobiologie, CNRS URA 1857, 46 rue d'Ulm, 75005 Paris, France;Unité des Venins, Institut Pasteur, 28 rue du Dr Roux, 75015 Paris, France;CEA, Service de Pharmacologie et d'Immunologie, DRM, CE Saclay, 91191 Gif sur Yvette cedex, France

关键词: Acetylcholinesterase;    Snake venom;    Bungarus fasciatus;    AChE;    acetylcholinesterase;    BChE;    butyrylcholinesterase;    AcSCh;    acetylthiocholine;    BuSCh;    butyrylthiocholine;    IEF;    isoelectric focusing;    PAGE;    polyacrylamide gel electrophoresis;    PIPLC;    phosphatidylinositol specific phospholipase C;    PrSCh;    propionylthiocholine;   

DOI  :  10.1016/0014-5793(96)00447-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown