Title : [Catalytic properties of cholinesterases immobilized in a gelatin membrane] - Kuznetsova_1990_Ukr.Biokhim.Zh_62_42
Author(s) : Kuznetsova LP , Kugusheva LI , Nikol'skaia EB
Ref : Ukr Biokhim Zh , 62 :42 , 1990
Abstract :

Catalytic properties of human blood erythrocyte acetylcholinesterase and horse blood serum butyrylcholinesterase immobilized and nonimmobilized in the gelatin membrane have been comparatively studied. Cholinesterase immobilization induces an increase in the Michaelis constant value and a decrease in the maximum rate value in reactions of enzymic hydrolysis of thiocholine ethers, but exerts no effect on these kinetic parameters in case of enzymic hydrolysis of indophenylacetate. The effect of reversible inhibitors: galanthamine, N-methyl-4-piperidinyl benzylate and 1,2,3,4-tetrahydro-9-aminoacridine (tacrine), as well as of irreversible inhibitors: O-ethyl-O-(4-nitrophenyl)ethyl phosphonate (armin), diisopropyl fluorophosphate (DFP), O,O-diethyl-O-(4-nitrophenyl) phosphate (paraoxon) and O,O-dimethyl-O-(2,2-dichlorovinyl) phosphate (DDVP) on immobilized cholinesterases is weaker as compared with the effect on nonimmobilized enzymes. The results obtained are discussed for the effect of immobilization on the catalytically active enzyme surface.

PubMedSearch : Kuznetsova_1990_Ukr.Biokhim.Zh_62_42
PubMedID: 2087792

Related information

Inhibitor Armin    DFP    Dichlorvos    Galanthamine    Paraoxon

Citations formats

Kuznetsova LP, Kugusheva LI, Nikol'skaia EB (1990)
[Catalytic properties of cholinesterases immobilized in a gelatin membrane]
Ukr Biokhim Zh 62 :42

Kuznetsova LP, Kugusheva LI, Nikol'skaia EB (1990)
Ukr Biokhim Zh 62 :42