@article{ref1,
title="Purification and characterization of acetylcholinesterase from desert cobra (Walterinnesia aegyptia) venom",
journal="Biochimie",
year="1996",
author="Duhaiman, A. S. and Alhomida, A. S. and Rabbani, N. and Kamal, M. A. and al-Jafari, A. A.",
volume="78",
number="1",
pages="46-50",
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.<p /><p>Language: en</p>",
language="en",
issn="0300-9084",
doi="",
url="http://dx.doi.org/"
}