Abstract
No catalase activity was detected in four strains of glucose-grown Mycoplasma pneumoniae at any time during the replication of the organism. Exogenous catalase dramatically increased the O2 uptake with glycerol, presumably by releasing inhibition caused by hydrogen peroxide. The effect of added catalase on the O2 uptake of washed organisms with glucose as substrate was moderate and variable in degree. The production of hydrogen peroxide was demonstrated by the quantitative enzymatic assay for inorganic peroxide and by the fact that added pyruvate, which is non-enzymatically oxidized by H2O2 to acetic acid and CO2 could mimic the action of catalase.
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