A hydrophobic dimer of acetylcholinesterase from Torpedo californica electric organ is solubilized by phosphatidylinositol-specific phospholipase C.
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.
D000110:Acetylcholinesterase; D000818:Animals; D002384:Catalysis; D004557:Electric Organ / Q000201:enzymology*; D010716:Phosphatidylinositols; D010740:Phospholipases; D011978:Receptors, Nicotinic; D012995:Solubility; D013211:Staphylococcus aureus / Q000201:enzymology; D013379:Substrate Specificity; D014101:Torpedo; D010738:Type C Phospholipases
D010716:Phosphatidylinositols; D011978:Receptors, Nicotinic; D010740:Phospholipases; D000110:Acetylcholinesterase; D010738:Type C Phospholipases