| Title : A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C - Inestrosa_1988_Neurosci.Lett_90_186 |
| Author(s) : Inestrosa NC , Fuentes ME , Anglister L , Futerman AH , Silman I |
| Ref : Neuroscience Letters , 90 :186 , 1988 |
|
Abstract :
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. |
| PubMedSearch : Inestrosa_1988_Neurosci.Lett_90_186 |
| PubMedID: 3412641 |
Inestrosa NC, Fuentes ME, Anglister L, Futerman AH, Silman I (1988)
A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C
Neuroscience Letters
90 :186
Inestrosa NC, Fuentes ME, Anglister L, Futerman AH, Silman I (1988)
Neuroscience Letters
90 :186