Characterization of the Peroxidase in Human Eosinophils

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Abstract
1. Human eosinophils contain a peroxidase that appears to be of the same type as horseradish peroxidase, lactoperoxidase and intestine peroxidase. 2. Electron paramagnetic resonance spectra of human eosinophils show high‐spin ferric heme signals with rhombic symmetry (gx= 6.56, gy= 5.31 and gx= 6.33, gy= 5.59) for the heme group. Part of the more rhombic signal is due to catalase, whereas the other part is completely due to the peroxidase. In addition to these high‐spin heme compounds a low‐spin heme compound is detectable with g values (gx= 3.09, gy= 2.22 and gz= 1.48) characteristic of a bisimidazole heme iron complex. 3. The amount of heme iron derived from the eosinophil peroxidase, determined from electron paramagnetic spectra, is 13.2 × 10−17 mol/eosinophil. This is in good agreement with the pyridine hemochrome spectra which yield a value of 13.5 × 10−17 mol heme iron/eosinophil.

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