电鳐乙酰胆碱酯酶疏水膜锚定结构域中共价结合肌醇的鉴定。

Identification of covalently bound inositol in the hydrophobic membrane-anchoring domain of Torpedo acetylcholinesterase.

作者信息

Futerman A H, Low M G, Ackermann K E, Sherman W R, Silman I

出版信息

Biochem Biophys Res Commun. 1985 May 31;129(1):312-7. doi: 10.1016/0006-291x(85)91439-1.

Abstract

The hydrophobic, membrane-bound form of Torpedo acetylcholinesterase is specifically solubilized by a phosphatidylinositol-specific phospholipase C, suggesting that acetylcholinesterase is bound to the membrane via a direct and specific interaction with phosphatidylinositol (Futerman et al., Biochem. J. (1985) 226, 369-377). Here we demonstrate the presence of covalently bound inositol in the membrane-anchoring domain of purified Torpedo acetylcholinesterase. Upon removal of this domain, levels of inositol are reduced to only 15-20% of those found in the intact enzyme. The results presented strongly support our suggestion that phosphatidylinositol is indeed involved in anchoring acetylcholinesterase to the plasma membrane.

摘要

电鳐乙酰胆碱酯酶的疏水膜结合形式可被磷脂酰肌醇特异性磷脂酶C特异性溶解，这表明乙酰胆碱酯酶通过与磷脂酰肌醇的直接特异性相互作用与膜结合（Futerman等人，《生物化学杂志》（1985年）226卷，369 - 377页）。在此我们证明，纯化的电鳐乙酰胆碱酯酶的膜锚定结构域中存在共价结合的肌醇。去除该结构域后，肌醇水平降至完整酶中发现的水平的仅15 - 20%。所呈现的结果有力地支持了我们的观点，即磷脂酰肌醇确实参与将乙酰胆碱酯酶锚定到质膜上。