Hodgson A J, Chubb I W
J Neurochem. 1983 Sep;41(3):654-62. doi: 10.1111/j.1471-4159.1983.tb04791.x.
A single molecular form of soluble acetylcholinesterase was isolated from a variety of mammalian tissues by use of a novel affinity matrix. This matrix was synthesised by coupling the reversible cholinesterase inhibitor, edrophonium chloride, to epoxy-activated Sepharose. This simple synthesis produced a matrix which was exceptionally stable and had the novel property of selectively binding only one molecular form of acetylcholinesterase. Soluble proteins from a variety of mammalian tissues, including brain, adrenal glands, cerebrospinal fluid, and blood, were separated by centrifugation. These contained combinations of acetylcholinesterase (EC 3.1.1.7) and cholinesterase (EC 3.1.1.8), varying from a single form of acetylcholinesterase to multiple forms of both acetylcholinesterase and cholinesterase. The edrophonium-Sepharose matrix bound only one form of acetylcholinesterase. This form of acetylcholinesterase corresponded in molecular size and electrophoretic mobility to the unique form found in cerebrospinal fluid, i.e. secretory acetylcholinesterase. Cholinesterase was not bound to the matrix.
通过使用一种新型亲和基质，从多种哺乳动物组织中分离出了单一分子形式的可溶性乙酰胆碱酯酶。这种基质是通过将可逆性胆碱酯酶抑制剂氯化依酚氯铵偶联到环氧活化的琼脂糖上合成的。这种简单的合成方法产生了一种异常稳定的基质，它具有仅选择性结合一种分子形式的乙酰胆碱酯酶的新特性。通过离心分离了来自多种哺乳动物组织（包括脑、肾上腺、脑脊液和血液）的可溶性蛋白质。这些蛋白质包含乙酰胆碱酯酶（EC 3.1.1.7）和胆碱酯酶（EC 3.1.1.8）的组合，从单一形式的乙酰胆碱酯酶到乙酰胆碱酯酶和胆碱酯酶的多种形式不等。依酚氯铵-琼脂糖基质仅结合一种形式的乙酰胆碱酯酶。这种形式的乙酰胆碱酯酶在分子大小和电泳迁移率上与脑脊液中发现的独特形式相对应，即分泌型乙酰胆碱酯酶。胆碱酯酶不与该基质结合。
