Peroxidase: a novel pathway for chemical oxidation in human term placenta.

@article{Joseph1992PeroxidaseAN,
  title={Peroxidase: a novel pathway for chemical oxidation in human term placenta.},
  author={P. Joseph and K. Murthy and J. L. Nelson and A. Kulkarni},
  journal={Placenta},
  year={1992},
  volume={13 6},
  pages={
          545-54
        }
}
Hydrogen peroxide-dependent oxidation of xenobiotics in a crude fraction of human term placental membranes (nuclei, mitochondria and microsomes) was investigated. Guaiacol was employed as a model substrate. The rate of its oxidation was found to be dependent on the concentration of protein, H2O2 and the substrate as well as the pH of the buffer. Several other classical substrates for peroxidases from different sources viz. pyrogallol, benzidine, p-PDA, DMBD, ABTS, TMPD and TMBD and endogenous… Expand
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The sulfhydryl reagent, N-ethylmaleimide, which caused a marked increase in the activity of uterine peroxidase, provided only partial protection against inactivation during storage of CaCl2 extracts of this enzyme at low temperature. Expand
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