Abstract
A peroxide-resistant mutant (PR) was isolated from Proteus mirabilis using the hydrogen peroxide mutagenic property. Under the same conditions, resistance of mutant PR bacteria to H2O2 was 50 to 100 times greater than that of the wild type. The total amount of catalase produced by P. mirabilis PR was on the average 10 times greater than that of the wild type. When PR bacteria were subjected to high doses of H2O2 (150mM), the determination of catalasic activity in vivo increased; paradoxically, there was a net decrease in the activity of the solubilized catalase after the breakdown of the cells. The hypothesis of an enzyme transfer from the inside towards the periphery of the cells is discussed. The behavior of a membrane enzyme (L-phenylalanine oxidase) of the PR mutant shows that H2O2 may cause lesions way up to the internal membrane of bacteria.
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