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[利用金属螯合亲和色谱法从人红细胞中纯化乙酰胆碱酯酶]

[Purification of acetylcholinesterase from human erythrocytes using metal-chelate affinity chromatography].

作者信息

Il'ina A V, Bannikova G E, Varlamov V P, Agabekian R S

出版信息

Prikl Biokhim Mikrobiol. 1996 Jul-Aug;32(4):389-92.

PMID:8984476
Abstract

Acetylcholinesterase (AChE) was purified on columns with iminodiacetate Agarose charged with Cu2+, Zn2+, and Ni2+. The best results (a 14-fold purification and more than 30% activity yield) were obtained with Zn2+ used as a complex-forming metal. The preparation had a specific activity of approximately 7 U. Its purity was tested by polyacrylamide gel electrophoresis under denaturing conditions.

摘要

乙酰胆碱酯酶(AChE)在装填有Cu2+、Zn2+和Ni2+的亚氨基二乙酸琼脂糖柱上进行纯化。以Zn2+作为络合金属时获得了最佳结果(纯化了14倍,活性回收率超过30%)。该制剂的比活性约为7 U。在变性条件下通过聚丙烯酰胺凝胶电泳对其纯度进行了检测。

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