Affiliation:
1. Cancer Research Institute and Department of Medicine, University of California Medical Center, San Francisco, California 94122
Abstract
In the presence of hydrogen peroxide and either potassium iodide, sodium chloride, or potassium bromide, purified human myeloperoxidase was rapidly lethal to several species of
Candida
. Its candidacidal activity was inhibited by cyanide, fluoride, and azide, and by heat inactivation of the enzyme. A hydrogen peroxidegenerating system consisting of
d
-amino acid oxidase, flavine-adenine dinucleotide, and
d
-alanine could replace hydrogen peroxide in the candidacidal system. Horseradish peroxidase and human eosinophil granules also exerted candidacidal activity in the presence of iodide and hydrogen peroxide; however, unlike myeloperoxidase or neutrophil granules, these peroxidase sources were inactive when chloride replaced iodide. Cells of
Saccharomyces, Geotrichum
, and
Rhodotorula
species, and spores of
Aspergillus fumigatus
and
A. niger
were also killed by the combination of myeloperoxidase, iodide, and hydrogen peroxide. Peroxidases, functionally linked to hydrogen peroxide-generating systems, could provide phagocytic cells with the ability to kill many fungal species.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
205 articles.
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