Structural requirements for the inhibition of human monocyte carboxylesterase by organophosphorus compounds.

@article{Saboori1991StructuralRF,
  title={Structural requirements for the inhibition of human monocyte carboxylesterase by organophosphorus compounds.},
  author={A. M. Saboori and D. Lang and D. Newcombe},
  journal={Chemico-biological interactions},
  year={1991},
  volume={80 3},
  pages={
          327-38
        }
}
  • A. M. Saboori, D. Lang, D. Newcombe
  • Published 1991
  • Chemistry, Medicine
  • Chemico-biological interactions
  • Human blood monocyte carboxylesterase (CBE) is inhibited by a variety of organophosphorus compounds including arylphosphates and arylphosphites and some alkylphosphites. Triphenyl phosphate and triphenyl phosphite with Ki values of 8 x 10(-9) M and 4.8 x 10(-8) M, respectively, are the most potent inhibitors of this enzyme evaluated by this study. The arylphosphates vary in their capacity to inhibit carboxylesterase activity. Diphenyl phosphate with its strong negative charge is not a potent… CONTINUE READING
    60 Citations
    The mammalian carboxylesterases: from molecules to functions.
    • 626
    In vitro inhibition of lysine decarboxylase activity by organophosphate esters.
    • 11
    • PDF
    Biology of Monocyte-Specific Esterase
    • 32
    Affinities of organophosphate flame retardants to tumor suppressor gene p53: an integrated in vitro and in silico study.
    • 12
    • PDF
    Pharmacokinetics and molecular detoxication.
    • 76
    • PDF

    References

    SHOWING 1-10 OF 25 REFERENCES
    Triphenyl phosphite: in vivo and in vitro inhibition of rat neurotoxic esterase.
    • 26
    Degradation by rat tissues in vitro of organophosphorus esters which inhibit cholinesterase.
    • 14
    Human monocyte carboxylesterase. Purification and kinetics.
    • 39
    Biochemical and neuropathological assessment of triphenyl phosphite in rats.
    • 27