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- W2053857826 abstract "Summary 1. Eosinophils, substantially free from neutrophils, have been obtained from the peritoneal cavity of rats. A haemoprotein has been extracted from the eosinophils at pH 3.7 and partially purified. 2. Kinetic studies of the catalysed reaction of hydrogen peroxide with guaiacol show that the haemoprotein is a true peroxidase (donor: H2O2 oxidoreductase, EC 1.11.1.7), k1 being approx. 5.0 · 106 M−1 sec−1 and Km (H2O2) approx. 4.5 · 10−4 M. 3. The oxidized and reduced forms of eosinophil peroxidase have spectra of the same type as horse-radish and milk peroxidases; the spectrum of the reduced form is different from that of reduced myeloperoxidase. 4. It is concluded that myeloperoxidase is present in blood only in neutrophils, and might be better termed “neutrophil peroxidase”, and that eosinophil peroxidase is a different enzyme. 5. The position of the a band of the pyridine haemochrome (567 mμ) formed from eosinophil peroxidase suggests that the prosthetic group is not protohaem." @default.
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- W2053857826 date "1965-01-01" @default.
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- W2053857826 title "Studies on rat eosinophil peroxidase" @default.
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- W2053857826 doi "https://doi.org/10.1016/s0926-6593(65)80010-8" @default.
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