Interaction of human red cell membrane acetylcholinesterase with phospholipids.
Liposomes of phospholipids fully sustain the enzyme activity of the amphiphile-dependent dimers of human erythrocyte membrane acetylcholinesterase; no head group specificity exists. Diacylglycerides, glycerophosphorylcholine, or free fatty acids do not sustain the catalytic activity. It could be shown that the dimeric acetylcholinesterase with an exposed hydrophobic region can penetrate the lipid bilayer of liposomes and thus becomes stabilized by the surrounding phospholipid molecules.
D000110:Acetylcholinesterase / Q000097:blood*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008081:Liposomes; D008563:Membrane Lipids / Q000097:blood; D010741:Phospholipases A / Q000494:pharmacology; D010743:Phospholipids / Q000097:blood / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D010738:Type C Phospholipases / Q000494:pharmacology
D008081:Liposomes; D008563:Membrane Lipids; D010743:Phospholipids; D010741:Phospholipases A; D000110:Acetylcholinesterase; D010738:Type C Phospholipases