MEDIATION OF p-AMINODIPHENYLAMINE OXIDATION VIA CYTOCHROME OXIDASE | Zendy

Philip Person | Zendy; M. S. Burstone | Zendy; Albert S. Fine | Zendy

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MEDIATION OF p-AMINODIPHENYLAMINE OXIDATION VIA CYTOCHROME OXIDASE

Author(s) -

Philip Person,

M. S. Burstone,

Albert S. Fine

Publication year - 1962

Publication title -

journal of histochemistry and cytochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.971

H-Index - 124

eISSN - 1551-5044

pISSN - 0022-1554

DOI - 10.1177/10.1.75

Subject(s) - cyanide , cytochrome c oxidase , chemistry , reagent , oxidase test , cytochrome , cytochrome c , pigment , enzyme , biochemistry , photochemistry , nuclear chemistry , organic chemistry , mitochondrion

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.

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