Purification and characterization of acetylcholinesterase from the Lake Van fish (Chalcalburnus tarichii Pallas, 1811)
Preparative Biochemistry and Biotechnology, vol.33, no.2, pp.137-145, 2003 (Scopus)
- Publication Type: Article / Article
- Volume: 33 Issue: 2
- Publication Date: 2003
- Doi Number: 10.1081/pb-120021438
- Journal Name: Preparative Biochemistry and Biotechnology
- Journal Indexes: Scopus
- Page Numbers: pp.137-145
- Keywords: Acetylcholinesterase, Affinity chromatography, Purification, Van Lake Fish (Chalcalburnus tarichii P. 1811)
- Isparta University of Applied Sciences Affiliated: No
Abstract
In this study, acetylcholinesterase (ACHE; EC 3.1.1.7) was purified from plasma and erythrocytes in the Lake Van fish (Chalcalburnus tarichii P.1811) by affinity chromatography. Enzymatic activity was spectrophotometrically measured according to Ellman's method, at 412nm. Then, the optimal pH and temperature of the enzyme was determined. According to the results, the optimal pH and the optimum temperature were 8.0 and 25°C, respectively. In order to control the purification of the enzyme, sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was done. SDS-PAGE showed a single band for enzyme. The purification rates for plasma AChE and erythrocyte AChE are 3251.6 and 8500, respectively.