Abstract
Peroxidases are a group of enzymes that catalyze the oxidation of a variety of electron donors by hydrogen peroxide (H2O2). Among the members of the group discussed at this meeting are myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). Although there are significant structural and functional similarities among members of the peroxidase family (see Chap.15), each of these peroxidases has a highly specific and very restricted range of tissue expression (Table 1.1). This historical review focuses predominantly on MPO as a representative member of this family of enzymes and perhaps the most thoroughly studied of the animal peroxidases [1]. MPO is present in the neutrophil (or heterophil) at very high concentrations, making up as much as 5% of the dry weight of the cell. Lesser amounts are found in blood monocytes, but tissue macrophages are generally lacking MPO. The enzyme has been detected in the leukocytes of a wide range of vertebrate species and of those studied is absent only from chicken and goose.
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Clark, R.A. (2000). Peroxidases: A Historical Overview of Milestones in Research on Myeloperoxidase. In: Petrides, P.E., Nauseef, W.M. (eds) The Peroxidase Multigene Family of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-58314-8_1
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