Purification and characterization of acetylcholinesterase from the Lake Van fish (Chalcalburnus tarichii Pallas, 1811).
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 412 nm. 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 degrees C, respectively. In order to control the purification of the enzyme, sodium dodecyl-sulfate-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.
Aliriz
Serpil
S
Science and Arts Faculty, Department of Chemistry, Yuzuncu Yil University, Van, Turkey.
Turkoglu
Vedat
V
D000110:Acetylcholinesterase / Q000097:blood / Q000302:isolation & purification* / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D003530:Cyprinidae; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D013696:Temperature
D000110:Acetylcholinesterase