Myeloperoxidase (MPO) is stored within the azurophilic granules of leukocytes and found within circulating neutrophils, monocytes, and some tissue macrophages. A unique activity of MPO is its ability to use chloride as a cosubstrate with hydrogen peroxide to generate chlorinating oxidants such as hypochlorous acid, a potent antimicrobial agent. Cayman’s Myeloperoxidase Chlorination Assay provides a convenient fluorescence-based method for detecting the MPO chlorination activity in both crude cell lysates and purified enzyme preparations.
MPO also oxidizes a variety of substrates, including phenols and anilines, via the classic peroxidation cycle. The relative concentrations of chloride and the reducing substrate determine whether MPO uses hydrogen peroxide for chlorination or peroxidation.
The fact that circulating levels of MPO have been shown to predict risks for major adverse cardiac events and that levels of MPO-derived chlorinated compounds are specific biomarkers for disease progression, has attracted considerable interest in the development of therapeutically useful MPO inhibitors.
Assays based on measurement of chlorination activity are more specific for MPO than those based on peroxidase substrates because peroxidases generally do not produce hypochlorous acid.
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