[Estimation of the irreversible inhibition reaction rate constants and of the concentration of cholinesterase active sites under commensurable concentrations of enzyme and inhibitors].
Kinetic analysis of the interaction of butyrylcholinesterase and the phosphoorganic inhibitor GT-161 [(C2H2O)2P(O)SC2H4+N(CH3)2C6H5-1-] is carried out. Short time incubations of an enzyme and an inhibitor (1-3 sec), even under commensurable concentrations, were shown to enable the rate constants of irreversible enzyme inhibition to be calcualted by the formula for pseudomonomoleuclar reactions. A simple analytical method for the estimation of the enzyme active sites concentrations is proposed.
D001665:Binding Sites; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D002802:Cholinesterases / Q000378:metabolism; D007700:Kinetics; D008433:Mathematics; D009946:Organothiophosphorus Compounds / Q000494:pharmacology; D011485:Protein Binding; D013997:Time Factors
D002800:Cholinesterase Inhibitors; D009946:Organothiophosphorus Compounds; D002802:Cholinesterases