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Myeloperoxidase: Localization, Structure, and Function

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Book cover Blood Cell Biochemistry Volume 3

Part of the book series: Blood Cell Biochemistry ((BLBI,volume 3))

Abstract

Myeloperoxidase (MPO) is a heme-containing enzyme that, in the presence of peroxide and halide ions, is effective in killing various microorganisms; in addition, it exerts a wide variety of extracellular functions. Polymorphonuclear leukocytes (PMN) are the main source of this enzyme. MPO is a myeloid cell-specific enzyme whose synthesis is tightly regulated at the promyelocyte stage of differentiation of myeloid cells. This review will consider recent developments concerning the biochemical and molecular structure, biosynthesis and processing, and various possible functions of MPO.

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Authors and Affiliations

  1. Central Hematology Laboratory, University of Berne, Inselspital, Switzerland

    Andreas Tobler

  2. Division of Hematology/Oncology, UCLA School of Medicine, Los Angeles, California, 90024, USA

    H. Phillip Koeffler

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  1. Andreas Tobler
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  2. H. Phillip Koeffler
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  1. North East Thames Regional Transfusion Centre, Brentwood, Essex, England

    J. R. Harris

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Tobler, A., Koeffler, H.P. (1991). Myeloperoxidase: Localization, Structure, and Function. In: Harris, J.R. (eds) Blood Cell Biochemistry Volume 3. Blood Cell Biochemistry, vol 3. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3796-0_10

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  • DOI: https://doi.org/10.1007/978-1-4615-3796-0_10

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