ON THE ASSOCIATION OF TYROCIDINE WITH ACETYLCHOLINESTERASE
- 1 March 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 62 (3), 986-993
- https://doi.org/10.1073/pnas.62.3.986
Abstract
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.Keywords
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