Acetylcholinesterase from Bungarus venom: A monomeric species

被引：60

作者：

Cousin, X

Creminon, C

Grassi, J

Meflah, K

Cornu, G

Saliou, B

Bon, S

Massoulie, J

Bon, C

机构：

[1] INST PASTEUR, UNITE VENINS, F-75015 PARIS, FRANCE

[2] NEUROBIOL LAB, CNRS URA 1857, F-75005 PARIS, FRANCE

[3] CEA, CE SACLAY, SERV PHARMACOL IMMUNOL, F-91191 GIF SUR YVETTE, FRANCE

[4] INSERM, U419, F-44035 NANTES 01, FRANCE

来源：

FEBS LETTERS | 1996年 / 387卷 / 2-3期

关键词：

acetylcholinesterase; snake venom; Bungarus fasciatus;

D O I：

10.1016/0014-5793(96)00447-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：196 / 200

页数：5

共 17 条

[1] AMPHIPHILIC, GLYCOPHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C (PI-PLC)-INSENSITIVE MONOMERS AND DIMERS OF ACETYLCHOLINESTERASE [J].