Interaction of membrane-bound and solubilized acetylcholinesterase from human and bovine erythrocytes with organophosphorus inhibitors

Differences are found between the membrane-bound and soluble acetylcholinesterases of human and bovine erythrocytes when the enzyme interacts with organophosphoric inhibitors in the presence of acetylc choline and galantamine, a reverse inhibitor of acetylcholinesterase. In most cases prevention of...

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Bibliographic Details
Published in:	Ukrainskij biohimičeskij žurnal Vol. 58; no. 3; p. 13
Main Authors:	Kugusheva, L I, Rozengart, V I
Format:	Journal Article
Language:	Russian
Published:	Ukraine 01-05-1986
Subjects:	Acetylcholinesterase - blood Animals Cattle Cholinesterase Inhibitors - metabolism Cholinesterase Reactivators - pharmacology Erythrocyte Membrane - enzymology Humans In Vitro Techniques Organophosphorus Compounds - metabolism Solubility Species Specificity Structure-Activity Relationship
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Summary:	Differences are found between the membrane-bound and soluble acetylcholinesterases of human and bovine erythrocytes when the enzyme interacts with organophosphoric inhibitors in the presence of acetylc choline and galantamine, a reverse inhibitor of acetylcholinesterase. In most cases prevention of inhibition of the soluble enzyme activity necessitates a higher (2-3 times higher) concentration of the protecting agent than protection of the membrane-bound enzyme. Concentrations of acetylcholine and galantamine providing a 50% protection of the enzyme did not practically depend on the strength of the anticholinesterase action of organophosphoric inhibitors.
ISSN:	0201-8470