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
Biochimiejournal_title
Biochimieauthors
Duhaiman AS,Alhomida AS,Rabbani N,Kamal MA,al-Jafari AAdoi
10.1016/0300-9084(96)81328-9subject
Has Abstractpub_date
1996-01-01 00:00:00pages
46-50issue
1eissn
0300-9084issn
1638-6183pii
0300908496813289journal_volume
78pub_type
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