Biochemical properties of anti-inflammatory drugs. 8. Inhibition of histamine formation catalyzed by substrate specific mammalian histidine decarboxylases. Drug antagonism of aldehyde binding to protein amino groups.

@article{Skidmore1966BiochemicalPO,
  title={Biochemical properties of anti-inflammatory drugs. 8. Inhibition of histamine formation catalyzed by substrate specific mammalian histidine decarboxylases. Drug antagonism of aldehyde binding to protein amino groups.},
  author={Ian Frederick Skidmore and Michael Wellesley Whitehouse},
  journal={Biochemical pharmacology},
  year={1966},
  volume={15 12},
  pages={
          1965-83
        }
}
  • Ian Frederick Skidmore, Michael Wellesley Whitehouse
  • Published 1966
  • Chemistry, Medicine
  • Biochemical pharmacology
  • Abstract Kinetic studies have shown that a number of acidic anti-inflammatory drugs (salicylate, “Ibufenac”, phenylbutazone, Indomethacin and Flufenamic acid) inhibit histamine formation by competing with pyridoxal phosphate for the coenzyme binding site, believed to be a lysyl ϵ-amino group on mammalian histidine decarboxylase. Apparent inhibitor constants ( Ki's ) for these drugs were measured. These drugs also inhibited the binding of pyridoxal phosphate and 2,4,6-trinitro-benzaldehyde… CONTINUE READING

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