1964
DOI: 10.1016/0014-4827(64)90364-7
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Studies on the localization of intracellular catalase of mouse liver

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1965
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Cited by 12 publications
(3 citation statements)
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“…That catalase is not likely to be responsible for MEOS activity is indicated by its distribution. Most of the hepatic catalase is localized in the cytosol and "mitochondria" (14). These fractions had negligible ethanol-oxidizing activity under our assay conditions for MEOS measurement.…”
mentioning
confidence: 81%
“…That catalase is not likely to be responsible for MEOS activity is indicated by its distribution. Most of the hepatic catalase is localized in the cytosol and "mitochondria" (14). These fractions had negligible ethanol-oxidizing activity under our assay conditions for MEOS measurement.…”
mentioning
confidence: 81%
“…mOCHEMISTRY: From equilibrium density measurements made in various concentrations of sucrose, Beaufay and Berthet (7) have come to the conclusion that the particles containing urate oxidase, catalase, and D-amino acid oxidase are essentially permeable to sucrose and should not be expected to respond osmotically to changes in sucrose concentration. Further support for this view has been obtained recently in experiments showing that catalase and D-amino acid oxidase are released to only a small extent from particles exposed to distilled water, although other treatments such as mechanical damage or exposure to surface-active agents readily liberate the enzymes in soluble form (2,17). These observations suggested that treatment of a mitochondrial fraction with distilled water may lead to a rather selective preservation of the particles containing urate oxidase, catalase, and D-amino acid oxidase and thus allow them to be separated more easily from mitochondria and lysosomes.…”
Section: Preparationmentioning
confidence: 92%
“…The identification of the microbodies as the bearers of urate oxidase, catalase, and D-amino acid oxidase receives particularly strong confirmation from the observations made on the watertreated preparation 3. It has been inferred from biochemical results that the particles containing the three enzymes are permeable to sucrose (7) and are not severely damaged by exposure to distilled water, as witnessed by the fact that this treatment does not release catalase or D-amino acid oxidase in appreciable quantities (2,17). This treatment has indeed allowed the separation of a purified fraction with a relatively high biochemical integrity index, and it is certainly striking that the microbodies, which are very numerous in this preparation, show relatively minor structural alterations.…”
Section: Microbodies As Sites Of Urate Oxidase Catalase and D-aminomentioning
confidence: 99%