Citation

Duhaiman AS, Alhomida AS, Rabbani N, Kamal MA, al-Jafari AA. Biochimie 1996; 78(1): 46-50.

Affiliation

Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia.

Copyright

(Copyright © 1996, Elsevier Publishing)

DOI

unavailable

PMID

8725010

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.

Language: en