Abstract
The bimolecular rate constants for the inhibition of bovine erythrocyte Cholinesterase by dimethyl-2-methoxycarbonyl-1-methyl vinyl phosphate (phosdrin), dimethyl-3-methyl-4-nitrophenyl phosphate (Sumioxon), dimethyl-2,2-dichlorovinyl phosphate (DDVP), and dimethyl-2-chloro-2-diethylcarbamoyl-1-methyl vinyl phosphate (phosphamidon) are 1.36 × 105, 4.02 × 104, 1.56 × 104, and 6.30 × 102 1/mole per minute, respectively, at 37°. The inhibition reaction involves reversible complex formation followed by phosphorylation of the enzyme. The values of the complexing constant for phosdrin, Sumioxon, and phosphamidon are 6.90 ± 0.82 × 10−5, 1.38 ± 0.21 × 10−4, and 1.90 ± 0.50 × 10−2 M, respectively. The respective phosphorylation constants are 9.24, 5.58, and 9.36 min−1.
Publisher
Canadian Science Publishing
Cited by
13 articles.
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