JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Klebanoff, S. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klebanoff, S. J.

 Previous Article  |  Next Article 

J Bacteriol. 1968 June; 95(6): 2131-2138
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Myeloperoxidase-Halide-Hydrogen Peroxide Antibacterial System

Seymour J. Klebanoff

1 U.S. Public Health Service Hospital, Seattle, Washington 98114; and the Research Training Unit, Department of Medicine, University of Washington, Seattle, Washington 98105

ABSTRACT

An antibacterial effect of myeloperoxidase, a halide, such as iodide, bromide, or chloride ion, and H2O2 on Escherichia coli or Lactobacillus acidophilus is described. When L. acidophilus was employed, the addition of H2O2 was not required; however, the protective effect of catalase suggested that, in this instance, H2O2 was generated by the organisms. The antibacterial effect was largely prevented by preheating the myeloperoxidase at 80 C or greater for 10 min or by the addition of a number of inhibitors; it was most active at the most acid pH employed (5.0). Lactoperoxidase was considerably less effective than was myeloperoxidase when chloride was the halide employed. Myeloperoxidase, at high concentrations, exerted an antibacterial effect on L. acidophilus in the absence of added halide, which also was temperature- and catalase-sensitive. Peroxidase was extracted from intact guinea pig leukocytes by weak acid, and the extract with peroxidase activity had antibacterial properties which were similar, in many respects, to those of the purified preparation of myeloperoxidase. Under appropriate conditions, the antibacterial effect was increased by halides and by H2O2 and was decreased by catalase, as well as by cyanide, azide, Tapazole, and thiosulfate. This suggests that, under the conditions employed, the antibacterial properties of a weak acid extract of guinea pig leukocytes is due, in part, to its peroxidase content, particularly if a halide is present in the reaction mixture. A heat-stable antibacterial agent or agents also appear to be present in the extract.


J Bacteriol. 1968 June; 95(6): 2131-2138
Copyright © 1968 American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1968 by the American Society for Microbiology. All rights reserved.