Myeloperoxidase: Localization, Structure, and Function

  • Andreas Tobler
  • H. Phillip Koeffler
Part of the Blood Cell Biochemistry book series (BLBI, volume 3)


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.


Acute Promyelocytic Leukemia Lysosomal Enzyme Human Neutrophil Chronic Granulomatous Disease Levulinic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • Andreas Tobler
    • 1
  • H. Phillip Koeffler
    • 2
  1. 1.Central Hematology LaboratoryUniversity of BerneInselspitalSwitzerland
  2. 2.Division of Hematology/OncologyUCLA School of MedicineLos AngelesUSA

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