A comparative study of the effect of vinyl phosphoric acid esters on cholinesterase and carboxylesterase activities in mammals and arthropods

Studies have been made of the effect of organophosphorus inhibitors on cholinesterase and carboxylesterase from various mammals (human erythrocytes, mouse brain, blood serum of mouse and rat, blood serum of horse) and arthropods (Calliphora vicina, Schizaphis graminum, Myzus persicae, Sitophilus ory...

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Bibliographic Details
Published in:	Žurnal ėvolûtsionnoj biohimii i fiziologii Vol. 26; no. 1; p. 30
Main Authors:	Kugusheva, L I, Rozengart, V I, Kozenasheva, L Ia, Kolesova, V A
Format:	Journal Article
Language:	Russian
Published:	Russia (Federation) 01-01-1990
Subjects:	Animals Arthropods - enzymology Carboxylic Ester Hydrolases - metabolism Chemical Phenomena Chemistry, Physical Cholinesterase Inhibitors - pharmacology Cholinesterases - metabolism Humans Insecticides - pharmacology Mammals - metabolism Mice Organophosphates - pharmacology Organophosphorus Compounds - pharmacology Rats Species Specificity Structure-Activity Relationship
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Summary:	Studies have been made of the effect of organophosphorus inhibitors on cholinesterase and carboxylesterase from various mammals (human erythrocytes, mouse brain, blood serum of mouse and rat, blood serum of horse) and arthropods (Calliphora vicina, Schizaphis graminum, Myzus persicae, Sitophilus oryzae, Pseudococcus maritimus, Tetranychus urticae). Organophosphorus inhibitors were presented by esters of vynylphosphoric acid containing normal and branched alkyls in the phosphoryl part of the molecule. The increase of the radical up to a propyl one increased the effect of organophosphorus inhibitors with respect to cholinesterase from the majority of the arthropods investigated. Organophosphorus compound with an isopropyl radical was found to be weaker for all the enzymes studied. Extremely high sensitivity of carboxylesterase from all arthropods to all organophosphorus inhibitors was noted; in some of the cases, anticarboxylesterase activity of all drugs was 2-3 orders higher than anticholinesterase one (P. maritimus, T. urticae). Regularities established for cholinesterase practically completely were confirmed on carboxylesterase. This finding evidently reveals similar structure of catalytic surface at the vicinity of esterase center in both enzymes.
ISSN:	0044-4529