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MEDIATION OF p-AMINODIPHENYLAMINE OXIDATION VIA CYTOCHROME OXIDASE

PHILIP PERSON 1, MARVIN S. BURSTONE 1, and ALBERT S. FINE 1

1 Special Dental Research Laboratory, V. A. Hospital, Brooklyn 28, N. Y., and the Diagnostic Research Branch, National Cancer Institute, Bethesda 14, Maryland

Manometric studies have revealed that the oxidation of p-aminodiphenylamine by Keilin and Hartree beef heart muscle particles was several-fold higher in the presence of added cytochrome c than in the absence of the pigment. The oxidation of p-aminodiphenylamine was inhibited 90% by 10–4 M cyanide. Correlated spectrophotometric studies demonstrated that the oxidation of p-aminodiphenylamine by Keilin and Hartree particles and fresh-frozen dehydrated tissue sections produced substances with identical visible and ultraviolet absorption spectra. The above experiments further indicate that the oxidation of p-aminodiphenylamine is mediated via cytochrome oxidase, and that this reagent provides valid histochemical localizations of the respiratory enzyme.

Submitted on June 30, 1961


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