A recent article by Winternitz and Meloy1 on the occurrence of catalase in human tissues, and its variations in diseases, leads us to review briefly the work already done with this ferment, especially on account of the possibilities of its clinical application.
Schoenbein observed in 1863 that aqueous extracts of various vegetable and animal tissues were capable of decomposing hydrogen peroxid with the evolution of oxygen, and ascribed this phenomenon to the various soluble ferments present in the organisms. The property was regarded as common to all enzymes until Loew, in 1901, showed that it belonged to a specific enzyme of universal occurrence in living organisms. This investigator succeeded in isolating this ferment from its companions and called it catalase. At first it was supposed that catalase played an active part in the oxidizing processes of the body, but the researches of Traube, and later those of Kastle and
THE CLINICAL SIGNIFICANCE OF QUANTITATIVE VARIATIONS IN CATALASE. JAMA. 1908;LI(21):1784. doi:10.1001/jama.1908.02540210040004
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