Brandan E, Inestrosa N C
Biochem J. 1984 Jul 15;221(2):415-22. doi: 10.1042/bj2210415.
The interaction between acetylcholinesterase (EC 3.1.1.7) and heparin, a sulphated glycosaminoglycan, was studied by affinity chromatography. A specific binding of the asymmetric acetylcholinesterase to an agarose gel containing covalently bound heparin was demonstrated. This interaction required an intact collagenous tail, shown by the fact that the binding is abolished by pretreatment with collagenase. The globular forms did not bind to the column. Both total and intracellular asymmetric acetylcholinesterase forms isolated from the endplate region of the rat diaphragm muscle showed higher affinity for the heparin than did the enzyme from the non-endplate region. The binding to the resin was destabilized with 0.55 M-NaCl, and, among the various glycosaminoglycans tested, only heparin was able to displace the acetylcholinesterase bound to the column. Our results added further support to the concept that the asymmetric acetylcholinesterase forms are immobilized on the synaptic basal lamina via interactions with heparin-like molecules, probably related to heparan sulphate proteoglycans.
通过亲和色谱法研究了乙酰胆碱酯酶（EC 3.1.1.7）与硫酸化糖胺聚糖肝素之间的相互作用。结果表明，不对称型乙酰胆碱酯酶与含有共价结合肝素的琼脂糖凝胶存在特异性结合。这种相互作用需要完整的胶原尾部，胶原酶预处理可消除结合这一事实证明了这一点。球状形式不与柱结合。从大鼠膈肌终板区域分离的总不对称型和细胞内不对称型乙酰胆碱酯酶对肝素的亲和力均高于非终板区域的酶。0.55 M氯化钠会使与树脂的结合不稳定，在所测试的各种糖胺聚糖中，只有肝素能够取代结合在柱上的乙酰胆碱酯酶。我们的结果进一步支持了以下概念：不对称型乙酰胆碱酯酶通过与类肝素分子（可能与硫酸乙酰肝素蛋白聚糖有关）的相互作用固定在突触基膜上。
