凡湖鱼类（Chalcalburnus tarichii Pallas，1811年）乙酰胆碱酯酶的纯化与特性分析

Purification and characterization of acetylcholinesterase from the Lake Van fish (Chalcalburnus tarichii Pallas, 1811).

作者信息

Aliriz Serpil, Turkoglu Vedat

机构信息

Science and Arts Faculty, Department of Chemistry, Yuzuncu Yil University, Van, Turkey.

出版信息

Prep Biochem Biotechnol. 2003 May;33(2):137-45. doi: 10.1081/PB-120021438.

DOI:10.1081/PB-120021438

PMID:12784884

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 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.

摘要

在本研究中，通过亲和层析从凡湖鱼（Chalcalburnus tarichii P.1811）的血浆和红细胞中纯化乙酰胆碱酯酶（AChE；EC 3.1.1.7）。根据埃尔曼方法，在412nm处通过分光光度法测量酶活性。然后，确定酶的最佳pH值和温度。根据结果，最佳pH值和最佳温度分别为8.0和25℃。为了控制酶的纯化，进行了十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）。SDS-PAGE显示酶为单一条带。血浆AChE和红细胞AChE的纯化率分别为3251.6和8500。