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. 1971 Apr;3(4):595–602. doi: 10.1128/iai.3.4.595-602.1971

Role of the Phagocyte in Host-Parasite Interactions XXVII. Myeloperoxidase-H2O2-Cl-Mediated Aldehyde Formation and Its Relationship to Antimicrobial Activity

R R Strauss 1, B B Paul 1, A A Jacobs 1, A J Sbarra 1
PMCID: PMC416202  PMID: 16558023

Abstract

Evidence is presented which suggests that the mechanism of action of the myeloperoxidase-H2O2-Cl antimicrobial system in the phagocyte is by the formation of aldehydes. Aldehyde production resulting from myeloperoxidase-mediated decarboxylation and deamination of alanine was quantitated with 20,000-g granules from guinea pig polymorphonuclear leukocytes serving as the enzyme. Equimolar quantities of acetaldehyde and CO2 were obtained. There was an absolute requirement for both H2O2 and Cl for decarboxylation by the myeloperoxidase-containing granules. The myeloperoxidase-H2O2-Cl system decarboxylated both d- or l-alanine equally and had a pH optimum of 5.3. Decarboxylation of l-alanine by intact guinea pig polymorphonuclear leukocytes was increased 2.5-fold by phagocytosis. Guaiacol peroxidation by the granules was inhibited 90% in the presence of Cl at acid pH. Under these conditions, decarboxylation and deamination of amino acids by myeloperoxidase were significantly stimulated, resulting in aldehyde production. Taurine, a competitive inhibitor of amino acid decarboxylation, inhibited bactericidal activity of the myeloperoxidase-H2O2-Cl system but had no effect on the myeloperoxidase-H2O2-I bactericidal system. Since the myeloperoxidase-H2O2-I system does not participate in amino acid decarboxylation, its mechanism of antimicrobial action appears to be different from that found with Cl.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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