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- W2018172021 abstract "Abstract The rates of spontaneous regeneration or decarbamylation of fly-head and bovine erythrocyte cholinesterase inhibited by methyl- and dimethylcarbamic acid esters were determined under different conditions of pH, salt concentrations, and temperature using Sephadex gel filtration as a means of isolating the carbamylated enzyme. The pH-rate profiles for decarbamylation of the two cholinesterases for both methyl- and dimethylcarbamylated enzyme had maximum rates at pH 8.5–8.9 for bovine erythrocyte and pH 8.1–8.5 for fly-head cholinesterase. Imidazole, hydroxylamine, and inorganic salts did not alter the decarbamylation rate. Values for the energy of activation for the decarbamylation reaction indicate a somewhat unstable and more reactive carbamylated enzyme for bovine cholinesterase compared to fly-head cholinesterase, but entropy factors are more favorable for decarbamylation in the latter. Regeneration rates in deuterium oxide for both enzymes and both methyl- and dimethylcarbamates were approximately six to seven times slower than in water, indicating a secondary isotope effect. A mechanism for decarbamylation consistent with the data is cited." @default.
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- W2018172021 date "1973-06-01" @default.
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- W2018172021 title "The reactivation of carbamate-inhibited cholinesterase, kinetic parameters" @default.
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- W2018172021 doi "https://doi.org/10.1016/0048-3575(73)90095-3" @default.
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