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XB-ART-27407
Neurosci Lett 1988 Jul 19;901-2:186-90. doi: 10.1016/0304-3940(88)90809-9.
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A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C.

Inestrosa NC , Fuentes ME , Anglister L , Futerman AH , Silman I .


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The susceptibility to phosphatidylinositol-specific phospholipase C of the membrane associated acetylcholinesterase (AChE) forms of Xenopus laevis skeletal muscle was examined. This treatment released almost all the detergent-soluble AChE species from muscle homogenates. Sucrose gradient analysis showed that the released acetylcholinesterase form corresponds to a hydrophilic G2 dimer, indicating that this dimer has a glycolipid anchoring domain which contains phosphatidylinositol.

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Species referenced: Xenopus laevis
Genes referenced: ache