Some properties of human eosinophil peroxidase, a comparison with other peroxidases.

@article{Bolscher1984SomePO,
  title={Some properties of human eosinophil peroxidase, a comparison with other peroxidases.},
  author={B G Bolscher and H Plat and Ron Wever},
  journal={Biochimica et biophysica acta},
  year={1984},
  volume={784 2-3},
  pages={177-86}
}
Eosinophil peroxidase (donor:hydrogen peroxide oxidoreductase, EC 1.11.1.7) was isolated from outdated human white blood cells. The purified enzyme has a molecular weight of 71000 +/- 1000. The enzyme is composed of two subunits, of Mr 58000 and 14000, in a 1:1 stoichiometry. Amino-acid analyses showed that eosinophil peroxidase has a high content of the amino acids arginine, leucine and aspartic acid. The millimolar absorbance coefficient of the Soret band at 412 nm of eosinophil peroxidase… CONTINUE READING

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