Effect of a hydrophobic interaction in the reaction of S-(β-alkylthioethyl) O-propyl methylphosphonothionates and their methyl methosulfates with cholinesterases of warm-blooded animals

Autor: Gulyamov, M., Tilyabaev, Z., Dalimov, D., Abduvakhabov, A.
Zdroj: Chemistry of Natural Compounds; September 1987, Vol. 23 Issue: 5 p579-582, 4p
Abstrakt: The action of S-(β-alkylthioethyl) O-propyl methylphosphonates and their methyl methosulfates with different lengths of the S-alkyl radical on the enzymatic activity of acetylcholinesterase from human blood erythrocytes and butyrylcholinesterase from horse blood serum has been investigated. The existence of a hydrophobic interaction on the sorption of inhibitors in the active site of the enzymes has been established. For the enzymes investigated a definite dependence has been observed of the antienzymatic activity of the compounds on the nature in the region of the anionic point and indicates differences in their length and structure.
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