Rakonczay Z, Brimijoin S
Biochim Biophys Acta. 1985 Nov 29;832(2):127-34. doi: 10.1016/0167-4838(85)90323-1.
Molecular forms of acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7) differ in their solubility properties as well as in the number of their catalytic subunits. We used monoclonal antibodies to investigate the structure of acetylcholinesterase forms in brain, erythrocytes and serum of rats, rabbits and other mammals. Two antibodies were found to bind tetrameric acetylcholinesterase in preference to the monomeric enzyme. These antibodies also displayed lower affinity for certain forms of 'soluble' brain acetylcholinesterase than for the 'membrane-associated' counterparts. Furthermore, one of them was virtually lacking in affinity for the membrane-associated enzyme of erythrocytes. The basis for the antibody specificity was not fully determined. However, the immunochemical results were supported by measurements of enzyme thermolability, which showed that the catalytic activity of 'soluble' acetylcholinesterase was comparatively heat-resistant. These observations point toward structural differences among the solubility classes of acetylcholinesterase.
乙酰胆碱酯酶（乙酰胆碱乙酰水解酶，EC 3.1.1.7）的分子形式在其溶解性以及催化亚基数量方面存在差异。我们使用单克隆抗体来研究大鼠、兔子及其他哺乳动物脑、红细胞和血清中乙酰胆碱酯酶形式的结构。发现两种抗体优先结合四聚体乙酰胆碱酯酶而非单体酶。这些抗体对某些形式的“可溶性”脑乙酰胆碱酯酶的亲和力也低于对“膜相关”对应物的亲和力。此外，其中一种抗体对红细胞的膜相关酶几乎没有亲和力。抗体特异性的基础尚未完全确定。然而，酶热稳定性的测量结果支持了免疫化学结果，该结果表明“可溶性”乙酰胆碱酯酶的催化活性相对耐热。这些观察结果表明乙酰胆碱酯酶溶解性类别之间存在结构差异。
