Abstract
AChE is the vital enzyme in the cholinergic nervous system. Hydrolysis of the Acetylcholine (ACh) in the nerve ending is the main function of this enzyme. By this way it maintains homeostasis of neurotransmitter in both central nervous
system and peripheral nervous system. In both pharmacological and toxicological way AChE provides a vital role. The aim of the study was to develop a simple protocol for the purification of Acetylcholinesterase enzyme (AChE) and to
extent an easy and worthy purification method for further characterization. The purification of AChE from bovine brain (Bostaurus) using gel chromatography on Sephadex G-200 was studied. The affinity matrix was synthesized by
coupling an inhibitor, acetate activated Sephadex G-200 with flow rate of 0.5ml/min. In this study the enzymes were purified 5 folds with aspecific activity of 18.95 UI/mg proteins.
system and peripheral nervous system. In both pharmacological and toxicological way AChE provides a vital role. The aim of the study was to develop a simple protocol for the purification of Acetylcholinesterase enzyme (AChE) and to
extent an easy and worthy purification method for further characterization. The purification of AChE from bovine brain (Bostaurus) using gel chromatography on Sephadex G-200 was studied. The affinity matrix was synthesized by
coupling an inhibitor, acetate activated Sephadex G-200 with flow rate of 0.5ml/min. In this study the enzymes were purified 5 folds with aspecific activity of 18.95 UI/mg proteins.
Original language | English |
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Pages (from-to) | 207-214 |
Number of pages | 8 |
Journal | International Journal of Pharmacy and Biological Sciences |
Volume | 5 |
Issue number | 2 |
Publication status | Published - 2015 |
Externally published | Yes |
Keywords
- Acetylcholinesterase
- Enzyme purification
- Bovine brain
- Gel chromatography
- Sephadex G-200