Purification of Cu, Zn-Superoxide Dismutase Isoenzymes from Fish Liver: Appearance of New Isoforms as a Consequence of Pollution

References

• Fridovich I. Superoxide dismutases. Annual Review of Biochemistry 1975; 44: 147–159
   PubMed Web of Science ®Google Scholar
• Chang L.-Y., Slot J. W., Geuze H. J., Crapo J. D. Molecular immunocytochemistry of the Cu,Zn-superoxide dismutase in rat hepatocytes. Journal of Cell Biology 1988; 107: 2169–2179
   PubMed Web of Science ®Google Scholar
• Keller G.-A., Warner T. G., Steimer K. S., Hallewell R. A. Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells. Proceedings of the National Acadamy of Sciences of USA 1991; 88: 7381–7385
   PubMed Web of Science ®Google Scholar
• Slot J. W., Geuze H. J., Freeman B. A., Crapo J. D. Intracellular localization of the copperzinc and manganese superoxide dismutases in rat liver parenchymal cells. Laboratory Investigation 1986; 55: 363–371
   PubMed Web of Science ®Google Scholar
• Sies H. Biochemistry of oxidative stress. Angewandte Chemie International Edition in English 1986; 25: 1058–1071
   Web of Science ®Google Scholar
• Yim M. B., Chock P. B., Stadtman E. R. Copper-zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proceedings of the National Academy of Sciences of USA 1990; 87: 5006–5010
   PubMed Web of Science ®Google Scholar
• Levine R. L. Oxidative modification of glutamine sinthetase. Journal of Biological Chemistry 1983; 258: 11823–11827
   PubMed Web of Science ®Google Scholar
• Buhler D. R., Williams D. E. The role of biotransformation in the toxicity of chemicals. Aquatic Toxicology 1988; 11: 19–28
   Web of Science ®Google Scholar
• Livingstone D. R. Towards a specific index of impact by organic pollution for marine invertebrates. Comparative Biochemistry and Physiology 1991; 100C: 151–155
   Google Scholar
• Winston G. W., Di Giulio R. T. Prooxidant and antioxidant mechanisms in aquatic organisms. Aquatic Toxicology 1991; 19: 137–161
   Web of Science ®Google Scholar
• Rodriguez-Ariza A., Abril N., Navas J. I., Dorado G., López-Barea J., Pueyo C. Metal, mutagenicity, and biochemical studies on bivalve molluscs from Spanish coasts. Environmental Molecular Mutagenesis 1992; 19: 112–124
   PubMed Web of Science ®Google Scholar
• Rodriguez-Ariza A., Dorado G., Peinado J., Pueyo C., López-Barea J. Biochemical effects of environmental pollution in fishes from Spanish South-Atlantic littoral. Biochemical Society Transactions 1991; 19: 301S
   PubMed Web of Science ®Google Scholar
• Martinez-Lara E., Pascual P., Toribio F., López-Barea J., Bárcena J. A. A rapid method for the quantification of glutathione transferase isoenzymes in crude extracts. Journal of Chroma-tography 1992; 609: 141–146
   PubMed Web of Science ®Google Scholar
• Lönnerdal B., Kee C. L., Hurley L. S. Isoelectric focusing of superoxide dismutase isoenzymes. FEBS Letters 1979; 108: 51–55
   PubMed Web of Science ®Google Scholar
• Crosti N., Sausa P. Evidence for tissue-specific electromorphs of Cu/Zn-SOD unrelated to genetic control. Biochemical Genetics 1980; 18: 693–697
   PubMed Web of Science ®Google Scholar
• Yano S. Multiple isoelectric variants of copper, zinc-superoxide dismutase from rat liver. Archives of Biochemistry and Biophysics 1990; 279: 60–69
   PubMed Web of Science ®Google Scholar
• Davies K. J.A. Protein damage and degradation by oxygen radicals. Journal of Biological Chemistry 1987; 262: 9895–9901
   PubMed Web of Science ®Google Scholar
• Salo D. C., Pacifici R. E., Lin S. W., Giulivi C., Davies K. J.A. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation. Journal of Biological Chemistry 1990; 265: 11919–11927
   PubMed Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural protein during the assembly of the head of bacterio-phage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Beauchamp C. O., Fridovich I. Superoxide dismutase improved assays and an assay applicable to acrylamide gels. Analytical Biochemistry 1971; 44: 276–287
   PubMed Web of Science ®Google Scholar
• Heukeshoven J., Dernick R. Simplified method for silver staining of proteins in poly-acrylamide gels and the mechanism of silver staining. Electrophoresis 1985; 6: 103–112
   Web of Science ®Google Scholar
• Lowry O. H., Rosebrough M. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagents. Journal of Biological Chemistry 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Smith P. K., Krohn R. I., Hermanson G. T., Mallia A. K., Gartner F. H., Provenzano M. D., Fujimoto E. K., Goeke N. M., Olson B. J., Klenk D. C. Measurement of protein using bicin-choninic acid. Analytical Biochemistry 1985; 150: 76–85
   PubMed Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase: an enzymic function for erythrocuprein. Journal of Biological Chemistry 1969; 244: 6049–6055
   PubMed Web of Science ®Google Scholar
• Jones G. L., Masters C. J. On the nature and characteristics of the multiple forms of catalase in mouse liver. Archives of Biochemistry and Biophysics 1975; 169: 7–21
   PubMed Web of Science ®Google Scholar
• Bueno P., del Río L. A. Purification and properties of glyoxysomal cuprozinc superoxide dismutase from watermelon cotyledons (Citrullus vulgaris Schrad). Plant Physiology 1992; 98: 331–336
   PubMed Web of Science ®Google Scholar
• Chance B., Boveris A., Nakase Y., Sies H. Hydroperoxide metabolism: an overview. Functions of glutathione in liver and kidney, H. Sies, A. Wendel. Springer-Verlag, Berlin, Heidelberg 1978; 95–106
   Google Scholar
• Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 1975; 14: 5294–5303
   Web of Science ®Google Scholar
• Ischiropoulos H., Zhu L., Chen J., Tsai M., Martin J. C., Smith C. D., Beckman J. S. Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Archives of Biochemistry and Biophysics 1992; 298: 431–437
   PubMed Web of Science ®Google Scholar