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. 1987 Jul 1;245(1):277–280. doi: 10.1042/bj2450277

Myeloperoxidase-dependent oxidative inactivation of neutrophil neutral proteinases and microbicidal enzymes.

M C Vissers 1, C C Winterbourn 1
PMCID: PMC1148111  PMID: 2822016

Abstract

The susceptibility of a number of human neutrophil granule enzymes to oxidative inactivation was investigated. Addition of H2O2 to the cell-free medium from stimulated neutrophils resulted in inactivation of all enzymes tested. This was inhibited by azide and methionine, indicating that inactivation was due to myeloperoxidase-derived oxidants. Lysozyme was more than 50% inactivated by one addition of 100 nmol of H2O2/ml, whereas myeloperoxidase, beta-glucuronidase, gelatinase and collagenase were almost completely inactivated by three additions. Cathepsin G was slightly less susceptible, whereas elastase was extremely resistant to oxidative attack. Myeloperoxidase-dependent enzyme inactivation may be a means whereby the neutrophil can terminate the activity of its granule enzymes and control the release of degradative enzymes into the tissues.

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Selected References

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