생쥐 뇌로부터 Triton X 100(10%)을 처리하여 AChE를 분리하고, DEAE-Sephacel 크로마토그래피 및 N-methylacridinium 친화성 크로마토그래피에 의해 효소를 부분정제 하였다. HPLC에 의한 부분정제된 AChE의 분자량을 측정한 결과, 339,000 및 609,000 dalton으로서 이 효소는 2종류의 회합된 형태로 존재함이 밝혀졌다. 계면활성제 처리 및 Concanavalin A 크로마토그래피 결과, 이 효소는 세포막에 소수성으로 결합된 당 단백질로서 밝혀졌다. 또한 최적 pH는 9.0, $K_m$ 값은 $46{mu}M$, 비활성도는 215.6 unit/mg으로 각각 밝혀졌으며 양이온성 소수성 화합물에 의해 강력히 저해됨이 관찰되었다.
Acetylcholinesterase (AChE) was solubilized from mouse brain membrane by 10% Triton X 100 treatment, and partially purified by DEAF-Sephacel chromatography plus affinity chromatography employing N-methylacridinium as the affinity ligand. The molecular weight of the partially purified enzyme was determined by high performance liquid chromatography (HPLC). It was revealed that the purified enzyme exists as two associated forms of molecular weight of 339,000 and 609,000. Concanavalin A affinity chromatography shows that this enzyme is a type of a hydrophobic glycoprotein that is bound to the membrane. $K_m$ value and specific activity of the purified enzyme which possessed the optimum pH of 9.0 were found to be $46{mu}M$ for acetylcholine and 215.6 units/mg, respectively. Inhibition studies show that the enzyme is inhibited strongly by hydrophobic compounds containing a cationic group.
