PMID: 5257018Mar 1, 1969Paper

On the association of tyrocidine with acetylcholinesterase

Proceedings of the National Academy of Sciences of the United States of America
J P ChangeuxT Podleski

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.

References

Feb 1, 1968·Biochemistry·R GoldmanE Katchalski
Jul 1, 1961·Biochemical Pharmacology·G L ELLMANR M FEATHER-STONE

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Citations

Jul 7, 1978·Biochimica Et Biophysica Acta·R K TripathiR D O'Brien
Jun 29, 1971·Biochimica Et Biophysica Acta·T Shafai, J A Cortner
Jan 1, 1974·Toxicon : Official Journal of the International Society on Toxinology·P A Nickerson, V Kumar
Sep 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·Y DudaiI Silman
Jun 7, 2011·Reviews in the Neurosciences·Claudio CoddouJ Pablo Huidobro-Toro
Sep 19, 1972·Biochimica Et Biophysica Acta·G Ciliv, P T Ozand
Dec 15, 1979·Journal of Molecular Biology·B Magdoff-Fairchild, J G White
Sep 5, 1975·Journal of Molecular Biology·C Chothia, W Leuzinger

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