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Biochem Biophys Res Commun. 1985 May 31;129(1):312-7.

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


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.

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