A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C.
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.
Inestrosa
N C
NC
Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.
Fuentes
M E
ME
Anglister
L
L
Futerman
A H
AH
Silman
I
I
D000110:Acetylcholinesterase / Q000493:pharmacokinetics*; D000818:Animals; D008565:Membrane Proteins / Q000493:pharmacokinetics; D009132:Muscles / Q000201:enzymology*; D012995:Solubility; D010738:Type C Phospholipases / Q000493:pharmacokinetics*; D014982:Xenopus laevis
D008565:Membrane Proteins; D000110:Acetylcholinesterase; D010738:Type C Phospholipases