[The effect of ionic strength on reversible inhibition of catalytic activity of acetylcholinesterase by thione phosphonates]. / Vliianie ionnoi sily na obratimoe tormozhenie kataliticheskoi aktivnosti atsetilkholinésterazy tionfosfonatami.
Ukr Biokhim Zh (1978)
; 61(4): 107-10, 1989.
Article
em Ru
| MEDLINE
| ID: mdl-2588333
ABSTRACT
The effect of ionic strength was used to analyze the mechanism of reversible acetylcholinesterase inhibition by three alkoxymethylthionphosphonates. The most considerable realization of the hydrophobic interaction with the surroundings of the enzyme esteratic site was marked for n-butyl derivative (compound I). The replacement of piperidine by morpholine (compound II) resulted in a decrease of the anticholinesterase activity by an order due to enhancement of the inhibitor hydrophilicity. An increase of MgCl2 concentration promotes an enhancement of the uncompetitive component contribution for compound III contrast to compound II. Hydrophobicity of the phosphoryl part of the compound I molecule is balanced under hydrophobic interaction of the heterocyclic "cationic head" with the enzyme anionic site. The break of this equilibrium intensifies the allosteric regulation, on the one hand, and lowers the inhibitor efficiency, on the other hand.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Compostos Organotiofosforados
/
Concentração Osmolar
/
Acetilcolinesterase
/
Inibidores da Colinesterase
Limite:
Humans
Idioma:
Ru
Ano de publicação:
1989
Tipo de documento:
Article