On the association of tyrocidine with acetylcholinesterase.

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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

Tyrothricin

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Tyrothricin	Acetylcholinesterase	Protein	Humans	Unknown	Inhibitor	Details
Tyrothricin	Beta-galactosidase	Protein	Escherichia coli (strain K12)	Unknown	Inhibitor	Details