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Nyberg, Schuberth & Anggard (1953) found that about 61 % of the catalase activity was present in the mitochondrial fraction of rat liver and only about 3-7 % in the mitochondrial fractions of horse and guinea-pig liver. Greenfield & Price (1956) claimed that catalase is present mainly in the mitochondrial fraction of rat liver but that it is eluted rapidly from mitochondria by 0-25M-sucrose solution, which they used as the homogenizing medium. They also reported the isolation of catalase from rat-liver mitochondria and showed that elution of catalase from mitochondria could be prevented by adding either polyvinylpyrrolidone or albumin to the homogenizing medium. Ludewig & Chanutin (1950), however, noted that about 45 % of the catalase activity of rat liver is present in mitochondria. Thomson & Klipfel (1957) reported that, during density-gradient centrifugation, ratliver catalase and uricase sediment closely together in a particulate fraction that is lighter than the particles containing succinate dehydrogenase and cytochrome oxidase, the enzyme markers for mitochondria. de Duve, Beaufay, Jacques, Rahman-Li & SelHinger (1960) observed a close relationship in the sedimentation properties of particles containing uricase, catalase and D-amino acid oxidase, and suggested that these enzymes are present in subcellular particles distinct from both mitochondria and lysosomes. de Duve, Wattiaux & Baudhuin (1962) point out that the prevention of elution of catalase from ratliver mitochondria by polyvinylpyrrolidone could be an absorption artifact, since the addition of polyvinylpyrrolidone to 0-25M-sucrose homogenates of rat liver containing a high proportion of soluble catalase also decreased the amount of enzyme present in the supernatant fraction. Intracellular redistribution of catalase during the incubation of mouse-liver slices was found by Adams & Elizabeth (1956), Adams & Burgess (1958, 1959 a, b) and Adams (1960). Roodyn, Suttie & Work (1962) observed negligible rates of incorporation of 14C_ labelled amino acids into catalase, malate dehydrogenase and cytochrome c under optimum conditions for the incorporation of radioactive amino acids into mitochondria. These authors, however, suggested that their failure to incorporate radioactive amino acids into the soluble enzymes isolated from mitochondria could be explained if these enzymes are not truly mitochondrial, and they emphasized the necessity for a re-examination of the intracellular localization of these enzymes in liver. Peters & Higashi (1963) suggested that the mitochondrial catalase of rat liver has its origin in vesicles that sediment with a granular microsome fraction and that it is then transferred gradually to mitochondria. They also considered the possibility that enzymically inactive microsomal catalase is a precursor of active catalase. The present work was undertaken with a view to relating the intracellular localization of catalase to its biosynthesis in rat liver. The incorporation of 59Fe into catalase has been studied mainly to assess whether there is any direct participation of mitochondria in the biogenesis of catalase. A preliminary account of some of this work has been published (Radhakrishnan & Sarma, 1963).

Studies on the intracellular localization and incorporation of 59Fe into catalase in rat liver