On the association of tyrocidine with acetylcholinesterase.
In studies of several polypeptide antibiotics with a high affinity for a variety of biological membranes, tyrocidine was found to bind specifically to acetylcholinesterase, an enzyme localized in excitable membranes. Several other polypeptides tested were not bound. Tyrocidine reversibly inhibits acetylcholinesterase formed by homogeneous protein, but seems to have no effect on the activity of the enzyme bound to the eel electroplax membrane. This inhibition is accompanied by a reversible association of the soluble enzyme in to ordered and rapidly sedimenting aggregates of large molecular weight. Electron micrographs of acetylcholinesterase are shown which are consistent with the chemical evidence of the existence of four subunits.
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001665:Binding Sites; D002800:Cholinesterase Inhibitors; D004524:Eels; D066298:In Vitro Techniques; D008566:Membranes; D008854:Microscopy, Electron; D010455:Peptides / Q000494:pharmacology*; D013501:Surface-Active Agents
D000900:Anti-Bacterial Agents; D002800:Cholinesterase Inhibitors; D010455:Peptides; D013501:Surface-Active Agents