Multiplicity of Antioxidant Enzyme Catalase in Mouse Liver Cells

References

• Sun Y. Free radicals, antioxidant enzymes, and carcinogenesis. Free Radicals in Biology and Medicine 1990; 8: 583–599
   PubMed Web of Science ®Google Scholar
• Szatrowski T. P., Nathan C. F. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Research 1991; 51: 794–798
   PubMed Web of Science ®Google Scholar
• MacCann J., Choi E., Yamasakim E., Ames B. N. Detection of carcinogens as mutagens in the Salmonella/microsome test: Assay of 300 chemicals. Proceedings of National Academy of Science 1975; 72: 5135–5139
   PubMed Web of Science ®Google Scholar
• Cerutti P. A. Prooxidant states and tumor promotion. Science, 227 1985; 375–381
   Google Scholar
• Pryor W. A. The role of free radical reactions in biological system. Free Radicals in Biology, W. A. Pryor. Academic Press, New York 1976; 1: 50
   Google Scholar
• Sun Y., Oberley L. W., Elwell J. H., Sierra-River´a E. Antioxidant enzyme activities in normal and transformed mouse liver cells. International Journal of Cancer 1989; 44: 1028–1033
   PubMed Web of Science ®Google Scholar
• Sun Y., Oberley L. W., Oberley T. D., Elwell J. H., Sierra-Rivera E. Lowered antioxidant enzymes in spontaneously transformed embryonic mouse liver cells in culture. Carcinogenesis 1993; 14: 1457–1463
   PubMed Web of Science ®Google Scholar
• Sun Y., Colbum N. H., Oberley L. W. Depression of catalase gene expression after immortalization and transformation of mouse liver cells. Carcinogenesis 1993; 14: 1505–1510
   PubMed Web of Science ®Google Scholar
• Wayne L., Diaz G. A. Double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Analytical Biochemistry 1986; 157: 89–92
   PubMed Web of Science ®Google Scholar
• Loewen P. C., Switala J. Multiple catalases in. Bacillus subtilis. Journal of Bacteriology 1987; 169: 601–3607
   Web of Science ®Google Scholar
• Holme R. S., Masters C. J. On the tissue and sub cellular distribution of multiple forms of catalase in the rat. Biochemistry Biophysics Acta 1969; 91: 488–490
   Google Scholar
• Holmes R. S., Masters C. J. Species specific features of the distribution and multiplicity of mammlian liver catalase. Archieve Biochemistry Biophysics 1972; 148: 217–223
   PubMed Web of Science ®Google Scholar
• Holmes R. S., Masters C. J. Genetic control and ontogeny of microbody enzymes: A review. Biochemistry Genetics 1978; 16: 171–190
   PubMed Web of Science ®Google Scholar
• Jones G. L., Masters C. J. On the turnover and proteolysis of catalase in tissues of the guinea pig and acatalasemic mice. Archive Biochemistry Biophysics 1976; 173: 463–471
   PubMed Web of Science ®Google Scholar
• Crane D., Holmes R. S., Masters C. J. Proteolytic modification of mouse liver catalase. Biochemistry Biophysics Research Communication 1982; 104: 1567–1572
   PubMed Web of Science ®Google Scholar
• Percy M. E. Catalase: an old enzyme with a new role?. Canadian Journal of Biochemistry Cell Biology 1984; 62: 1006–1014
   PubMedGoogle Scholar
• Masters C., Pegg M., Crane D. On the multiplicity of the enzyme catalase in mammalian liver. Molecular Cellular Biochemistry 1986; 70: 113–120
   PubMed Web of Science ®Google Scholar
• de Craemer D., Van Maldergem I., Roels F. Hepatic ultra structure in congenital total lipodystrophy with special reference to peroxisomes. Ultra structure Pathology 1992; 16: 307–316
   PubMed Web of Science ®Google Scholar
• Wiemer E. A., Out M., Schelen A., Wanders R. J., Schutgens R. B. H., Bosch H. V. D., Tager J. M. Phenotypic heterogeneity in cultured skin fibroblasts from patients with disorders of peroxisome biogenesis belonging to the same complementation group. Biochemistry Biophysics Acta 1991; 1097: 232–237
   PubMedGoogle Scholar
• Yajima S., Suzuki Y., Shimozawa N., Yamaguchi S., Orii T., Fujiki Y., Osumi T., Hashimoto T., Moser H. W. Complementation study of peroxisome-deficient disorders by immuno fluorescence staining and characterization of fused cells. Human Genetics 1992; 88: 491–499
   PubMed Web of Science ®Google Scholar
• Schrader M., Baumgart E., Volkl A., Fahimi H. D. Heterogeneity of peroxisomes in human hepato-blastoma cell line HepG2. Evidence of distinct subpopulations. European Journal of Cell Biology 1994; 64: 281–294
   PubMed Web of Science ®Google Scholar
• Masters C., Crane D. Isozymes and the micro organization of organellar structure and function. Progress in Clinical Biology Research 1990; 344: 101–122
   PubMedGoogle Scholar
• Cohen G., Dembiec D., Marcus J. Measurement of catalase activity in tissue extracts. Analytical Biochemistry 1970; 34: 30–38
   PubMed Web of Science ®Google Scholar
• Lowry O. H., Rosebrough N. J., Farr A. L., Randal R. J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Woodbury W., Spencer A. K., Stahmann M. A. An improved procedure using ferricyanide for detecting catalase isozymes. Analytical Biochemistry 1971; 44: 301–305
   PubMed Web of Science ®Google Scholar
• Sun Y., Elwell J. H., Oberley L. W. A simultaneous visualization of the antioxidant enzymes glu-tathione peroxidase and catalase on polyacrylamide gels. Free Radical Research Communication 1988; 5: 67–74
   PubMed Web of Science ®Google Scholar
• Hedrick J. L., Smith A. J. Size and charge iso-mer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Archive Biochemistry Biophysics 1968; 126: 155–164
   PubMed Web of Science ®Google Scholar
• Hoffman H. A., Grieshaber C. K. Genetic studies of murine catalase, liver and erythrocyte catalase controlled by independent loci. Journal of Heredity 1974; 65: 277–279
   PubMedGoogle Scholar
• Gulati S., Singh A. K., Irazu C., Orak J., Rajagopalan P. R., Fitts C. T., Singh I. Ischemia-reperfusion injury: biochemical alterations in peroxisomes of rat kidney. Archive Biochemistry Biophysics 1992; 295: 90–100
   PubMed Web of Science ®Google Scholar