Crystalline bacterial catalase

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Abstract
The use of lysozyme in the study of intracellular bacterial enzymes and some phenomena noticed when lysozyme acted on concentrated bacterial suspensions were discussed. Using lysozyme to liberate the enzyme from the bacterial cell, catalase was isolated from Micrococcus lysodeik-ticus in crystalline form. Bacterial catalase was similar in many respects to the catalases of animal tissues. The crystalline enzyme contained about 1.1% hematin, identical with ordinary blood hematin. It differed from liver catalases, but resembled erythrocyte catalases in containing no verdohematin. Hematin content and ultracentrifugal data indicated a mol. wt. of about 230,000, with 4 hematin groups/mol. The catalytic activity was considerably higher than that of mammalian tissue catalases; the difference was attributed to the protein component of the enzyme.