Molecular mechanism of general anesthesia: III. Kinetic studies on erythrocyte ghost acetylcholinesterase.
General anesthetics inhibit erythrocyte membrane-bound acetylcholinesterase. Release of the membrane-bound enzyme by sonication into a soluble form induces a loss of sensitivity to anesthetics. Reconstitution of the solubilized enzyme with phospholipids restores its inhibition by anesthetics. The results suggest that anesthetic inhibition of acetylcholinesterase is mediated through the lipid bilayer.
D000110:Acetylcholinesterase / Q000378:metabolism; D000768:Anesthesia, General; D000777:Anesthetics / Q000494:pharmacology*; D000440:Butanols / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000201:enzymology; D004912:Erythrocytes / Q000187:drug effects*; D006801:Humans; D066298:In Vitro Techniques; D007649:Ketamine / Q000494:pharmacology; D008563:Membrane Lipids / Q000032:analysis; D008565:Membrane Proteins / Q000032:analysis; D010743:Phospholipids / Q000494:pharmacology; D011487:Protein Conformation / Q000187:drug effects
D000777:Anesthetics; D000440:Butanols; D008563:Membrane Lipids; D008565:Membrane Proteins; D010743:Phospholipids; D007649:Ketamine; D000110:Acetylcholinesterase