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  • Title: [Inhibition of the activity of human serum cholinesterase by aminoalkyl benzenesulfonyl fluorides].
    Author: Kleking GP, Markvardt F, Rikhter M.
    Journal: Farmakol Toksikol; 1976; 39(3):265-8. PubMed ID: 1026506.
    Abstract:
    Aminoalkyl benzenesulfonyl fluorides, like organophosphates, act as irreversible inhibitors of serine proteinases by splitting off hydrogen fluoride to form an enzyme-inhibitor complex, stable in the physiological pH region. Several of these compounds are characterized by a higher rate of inhibition when trypsin is used and the second order rate constants are compared with those of organophosphates. On the other hand, upon inhibition of human serum cholinesterase by DFP and 4-nitrophenyl diethyl phosphate, some orders of magnitude higher than that of benzenesul fonyl fluorydes are observed. As shown by an oral toxicity study in mice similar differences exist with respect to LD50 values.
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