On the association of tyrocidine with acetylcholinesterase.
Article Details
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Changeux JP, Ryter A, Leuzinger W, Barrand P, Podleski T
On the association of tyrocidine with acetylcholinesterase.
Proc Natl Acad Sci U S A. 1969 Mar;62(3):986-93.
- PubMed ID
- 5257018 [ View in PubMed]
- 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.
DrugBank Data that Cites this Article
- Drugs
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Tyrothricin Acetylcholinesterase Protein Humans UnknownInhibitorDetails Tyrothricin Beta-galactosidase Protein Escherichia coli (strain K12) UnknownInhibitorDetails