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MICRODETERMINATION OF CYTOCHROME OXIDASE IN RAT TISSUES BY THE OXIDATION OF N-PHENYL-p-PHENYLENEDIAMINE OR ASCORBIC ACID

W. PEARL 1, J. CASCARANO 1, and B. W. ZWEIFACH 1

1 Department of Pathology, New York University Medical Center, New York, N. Y.

The cytochrome oxidase content of rat tissues was investigated, utilizing the accumulation of the free radical formed by the emzymatic, univalent oxidation of a stable, non-toxic substrate, N-phenyl-p-phenylenediamine (p-aminodiphenylamine). This procedure eliminated the non-enzymatic coupling of the radical with agr-naphthol, found in the classic Nadi reaction. Using homogenates, the following decreasing order of enzyme activity was found: heart, kidney, diaphragm, liver, rectus abdominis. A more sensitive assay was also developed, involving the reduction of cytochrome c by ascorbic acid, and using 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyl tetrazolium chloride to analyze unoxidized ascorbic acid. The same order of tissue activity was demonstrated. The cytochrome oxidase content of a tissue may be a reflection of its physiological role.

Submitted on May 12, 1962


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