Peroxidatic activity of catalase
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چکیده
منابع مشابه
Peroxidatic activity of mycobacteria and relation to catalase.
Winder, Frank G. (Trinity College, Dublin, Ireland). Peroxidatic activity of mycobacteria and relation to catalase. J. Bacteriol. 92:413-417. 1966.-Catalase from Mycobacterium smegmatis was purified about 50-fold. All fractions showed a ratio of peroxidatic activity to catalatic activity approximately the same as that of the crude extract, a ratio only about four times that given by catalase fr...
متن کاملCytochemical Localization of Peroxidatic Activity of Catalase in Rat Hepatic Microbodies (peroxisomes)
Prominent staining of rat hepatic microbodies was obtained by incubating sections of aldehyde-fixed rat liver in a modified Graham and Karnovsky's medium for ultrastructural demonstration of peroxidase activity. The electron-opaque reaction product was deposited uniformly over the matrix of the microbodies. The microbodies were identified by their size, shape, presence of tubular nucleoids, and...
متن کاملSuperoxide dismutase, peroxidatic activity and catalase in Mycobacterium leprae purified from armadillo liver.
Superoxide dismutase has been identified and peroxidatic activity demonstrated in Mycobacterium leprae. The superoxide dismutase, shown indirectly to be a manganese-containing enzyme, was present at low activity in the cell-free extract. Peroxidatic activity was detected in a haemoprotein on polyacrylamide gels, but quantitative assay was not possible. Catalase, although present in a cell-free ...
متن کاملThe characteristics of the "peroxidatic" reaction of catalase in ethanol oxidation.
Ethanol oxidation by rat liver catalase (the ;peroxidatic' reaction) was studied quantitatively with respect to the rate of H(2)O(2) generation, catalase haem concentration, ethanol concentration and the steady-state concentration of the catalase-H(2)O(2) intermediate (Compound I). At a low ratio of H(2)O(2)-generation rate to catalase haem concentration, the rate of ethanol oxidation was indep...
متن کاملOn the oxidation of dihydrothiamine by the peroxidatic reaction of liver catalase.
As reported in the previous paper, dihydrothiamine (DHT), does not seem to be oxidized in biological systems by pyridine nucleotide enzymes or flavin enzymes in view of a high redox-potential of DHT (1). Its possible mecha nism, therefore, is assumed to be oxidation of DHT by a coupled oxidation at a terminal step of the respiratory system by a specific oxidase. Uehara's observation of the oxid...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1955
ISSN: 0306-3283
DOI: 10.1042/bj0610122