A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C

N C Inestrosa; M E Fuentes; L Anglister; A H Futerman; I Silman

doi:10.1016/0304-3940(88)90809-9

A membrane-associated dimer of acetylcholinesterase from Xenopus skeletal muscle is solubilized by phosphatidylinositol-specific phospholipase C

Neurosci Lett. 1988 Jul 19;90(1-2):186-90. doi: 10.1016/0304-3940(88)90809-9.

Authors

N C Inestrosa¹, M E Fuentes, L Anglister, A H Futerman, I Silman

Affiliation

¹ Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.

PMID: 3412641
DOI: 10.1016/0304-3940(88)90809-9

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Acetylcholinesterase / pharmacokinetics*
Animals
Membrane Proteins / pharmacokinetics
Muscles / enzymology*
Solubility
Type C Phospholipases / pharmacokinetics*
Xenopus laevis

Substances

Membrane Proteins
Acetylcholinesterase
Type C Phospholipases