References
- Bell G. I., Najarian R. C., Mullenbach G. T., Hallewell R. A. cDNA sequence coding for human kidney cata-lase. Nucleic Acids Res. 1986; 14: 5561–5562
- Cohen G., Hochstein P. Glutathione peroxidase: The primary agent for the elimination of hydrogen peroxide in erythroqte. Biochistry 1963; 2: 1420–1428
- Fita I., Rossmann M. G. The NADPH binding site on beef liver catalase. Proc. Natl. Acad. Sci. USA 1985; 82: 1604–1608
- Fita I., Rossmann M. G. The Active Center of Catalase. I. Mol. Biol. 1985; 185: 21–47
- Fwta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T., Hashimoto T. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc. Natl. Acad. Sci. USA 1986; 83: 313–317
- Kirkman H. N., Gaetani G. F. Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH. Proc. Natl. Acad. Sci. USA 1984; 81: 4343–4347
- Kirkman H. N., Galiano S., Gaetani G. F. The function of Catalase-bound NADPH. J Biol. Chem. 1987; 262: 660–666
- Lazarow P. B., Fujiki Y. Biogenesis of peroxisomes. Annu Rev. Cell Biol. 1985; 1: 489–530
- Nakamura K., Watanabe M., Sawai-Tanimoto S., Ikeda T. A Low Catalase Activity in Dog Erythrocytes is due to a Very Low Content of Catalase Protein despite Having a Normal Specific Activity. Int. J. Biochem. Cell Biol. 1998, in press
- Purdue P. E., Lazarow P. B. Targeting of Human Catalase to Peroxisome Is Dependent upon a Novel COOH-Terminal Peroxisomd Targeting Sequence. J. Cell Biol. 1996; l34: 849–862
- Richardson M., Huddleson I. F., Bethea R., Trustdorf M. Study of Catalase in Erythrocytes and Bacteria. XI. Catalase Activity of Erythrocytes from Different Species of Normal Animals and from Normal Humans. Arch. Biochon. Biophys 1953; 42: 124–134
- Schroeder W. A., Shelton J. R., Shelton J. B., Robberson B., Apell G., Fang RS., Bonaventura J. The Complete Amino Acid Sequence of Bovine Liver Catalase and the Partial Sequence of Bovine Erythrocyte Catalase. Arch. Biochem. Biophys 1982; 214: 397–421
- Shaffer J. B., Preston K. E. Molecular analysis of an acatalasemic mouse mutant. Biochem. Biophys. Res. Comm. 1990; 173: 1043–1050