Inhibition of myeloperoxidase by benzoic acid hydrazides.

@article{Kettle1995InhibitionOM,
  title={Inhibition of myeloperoxidase by benzoic acid hydrazides.},
  author={Anthony J Kettle and C A Gedye and Mark B Hampton and Christine C Winterbourn},
  journal={The Biochemical journal},
  year={1995},
  volume={308 ( Pt 2)},
  pages={559-63}
}
Myeloperoxidase is the most abundant protein in neutrophils and catalyses the conversion of H2O2 and chloride into HOCl. To help clarify the role of this enzyme in bacterial killing and inflammation, a specific and potent inhibitor needs to be identified. We have studied a series of benzoic acid hydrazides and found that in general they inhibit the peroxidation activity of myeloperoxidase with an IC50 value of less than 10 microM. The IC50 values of derivatives with substituents containing… CONTINUE READING