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A hydrophobic dimer of acetylcholinesterase from Torpedo californica electric organ is solubilized by phosphatidylinositol-specific phospholipase C.

Authors
  • Futerman, A H
  • Low, M G
  • Silman, I
Type
Published Article
Journal
Neuroscience Letters
Publisher
Elsevier
Publication Date
Sep 19, 1983
Volume
40
Issue
1
Pages
85–89
Identifiers
PMID: 6633970
Source
Medline
License
Unknown

Abstract

A dimeric form of acetylcholinesterase from the electric organ of Torpedo californica was solubilized by phosphatidylinositol-specific phospholipase C from Staphylococcus aureus. The solubilized enzyme had a sedimentation coefficient of 7.3S which was not modified by detergents. The high salt-soluble asymmetric forms of acetylcholinesterase were not solubilized by the phospholipase. Our data suggest that the hydrophobic dimer of acetylcholinesterase may be associated with the plasma membrane through a specific interaction involving phosphatidylinositol.

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