Sensitivity of erythrocyte acethylcholinesterase to inhibition by linolenoyl sorbitol. Dependence on a transmembrane potential.
Acetylcholinesterase activity of human erythrocytes is known to be inhibited by linolenoyl sorbitol, the inhibition being critically dependent on cell membrane intactness. The extent of enzyme inhibition by the added lipid is correlated with the magnitude of Cl- gradient across the erythrocyte membrane, indicating that enzyme sensitivity is associated with a transmembrane potential. If linolenoyl sorbitol is allowed to interact with the erythrocytes while a Cl- gradient exists, enzyme sensitivity can subsequently be demonstrated not only in the absence of a gradient but even when the cells are lyzed. It is consluded that the transmembrane potential determines the accessibility of a membrane component to the added lipid.
D000110:Acetylcholinesterase / Q000097:blood*; D002462:Cell Membrane / Q000502:physiology; D002712:Chlorides / Q000494:pharmacology; D002800:Cholinesterase Inhibitors; D004912:Erythrocytes / Q000187:drug effects / Q000201:enzymology* / Q000502:physiology; D006801:Humans; D007700:Kinetics; D008042:Linolenic Acids / Q000494:pharmacology*; D008564:Membrane Potentials; D009996:Osmotic Fragility / Q000187:drug effects; D012964:Sodium / Q000494:pharmacology; D012965:Sodium Chloride / Q000494:pharmacology; D013012:Sorbitol / Q000494:pharmacology*; D013431:Sulfates / Q000494:pharmacology
D002712:Chlorides; D002800:Cholinesterase Inhibitors; D008042:Linolenic Acids; D013431:Sulfates; D012965:Sodium Chloride; D013012:Sorbitol; D012964:Sodium; D000110:Acetylcholinesterase