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. 1978 Dec;22(3):672–675. doi: 10.1128/iai.22.3.672-675.1978

Enzymatic degradation of H2O2 by Leptospira.

R E Corin, E Boggs, C D Cox
PMCID: PMC422212  PMID: 730380

Abstract

The enzymes responsible for reducing H2O2 were surveyed in 49 strains of Leptospira by using semiquantitative assays for catalase and peroxidase. The survey revealed a differential distribution of catalase and peroxidase activities between the two leptospiral complexes. The pathogenic Leptospira interrogans strains gave strong catalase and weak or negative peroxidase reactions. Conversely, the nonpathogenic Leptospira biflexa strains gave strong peroxidase and negative or weak catalase reactions. An intermediate group of four L. biflexa strains, which were isolated from mammals, fell into the high peroxidase, low or negative catalase group. One water isolate, H-23, gave strong reactions for both enzymes and was examined for virulence and in vitro growth parameters. Results indicate metabolic differences between pathogens and water forms in their abilities to reduce H2O2.

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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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