Purification and characterization of acetylcholinesterase from desert cobra (Walterinnesia aegyptia) venom.

Abstract:

:Acetylcholinesterase (AChE) has been identified and purified from the venom of desert cobra (W aegyptia) to apparent homogeneity using a TSK G 3000 SW gel filtration column and a Mono Q anion-exchange column. AChE was purified to homogeneity as established by sodium dodecylsulfate/polyacrylamide gel electrophoresis. The specific activity of AChE was 357 IU/mg with acetylthiocholine iodide as substrate. The denatured W aegyptia venom AChE displayed a molecular mass of 67000 +/- 3000 Da suggesting it was a single polypeptide. Isoelectric focusing of AChE revealed that the enzyme exists in different isoforms, with isoelectric points ranging between pH 7.4-7.9. The kinetic parameters (Km and Vmax) and IC50 of AChE inhibition by procaine, tetracaine and physostigmine were investigated in the present study.

journal_name

Biochimie

journal_title

Biochimie

authors

Duhaiman AS,Alhomida AS,Rabbani N,Kamal MA,al-Jafari AA

doi

10.1016/0300-9084(96)81328-9

subject

Has Abstract

pub_date

1996-01-01 00:00:00

pages

46-50

issue

1

eissn

0300-9084

issn

1638-6183

pii

0300908496813289

journal_volume

78

pub_type

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