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Original Article

Changes in Superoxide Dismutase Activity in Liver and Lung of Old Rats

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Pages 401-405 | Received 10 Feb 1996, Published online: 07 Jul 2009

References

  • Stadtman E. R. Oxidation of proteins by mixed-function oxidation system: implication in protein turnover, aging and neutrophil function. Trends in Biochemical Sciences 1986; 11: 11–12
  • Halliwell B., Gutteridge J. M.C. Free Radicals in Biology and Medicine. Clarendon Press, Oxford 1989; 266–270
  • Harman D. Free radical theory of aging. Mutation Research 1992; 275: 257–266
  • McCord J. M. Superoxide dismutases: Occurrence, structure, function and evolution. In Current Topics in Biological and Medical Research, M. Rattazi, J. Scandalious, G. S. Whirl. Liss, New York 1979; vol. 3: 1–21
  • Machado A., Ayala A., Gordillo E., Revilla E., Santa Maria C. Relationship between enzymatic activity loss and post-translational protein modification in aging. Archives of Gerontology and Geriatrics 1991; 12: 187–197
  • Santa Maria C., Machado A. Changes in some hepatic enzyme activities related to phase II drug metabolism in male and female rats as a function of age. Mechanisms of Ageing and Development 1988; 44: 115–125
  • Gordillo E., Ayala A., Lobato M. F., Bautista J., Machado A. Possible involvement of histidine residues in the loss of enzymatic activity of rat liver malic enzyme during aging. Journal of Biological Chemistry 1988; 263: 8053–8057
  • Gordillo E., Ayala A., Bautista J., Machado A. Implication of lysine residues in the loss of enzymatic activity in rat liver 6-phosphogluconate dehydrogenase found in aging. Journal of Biological Chemistry 1989; 264: 17024–17028
  • Santa Maria C., Revilla E. A., Ayala de la Cruz C. P., Machado A. Changes in the histidine residues of Cu/Zn superoxide dismutase during aging. FEBS Letters 1995; 374: 85–88
  • Deneke S. M., Fanburg B. L. Oxygen toxicity of the lung: an update. British Journal of Anaesthesia 1982; 54: 737–742
  • McCord J. M., Fridovich I. Superoxide Dismutase. An enzymatic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry 1969; 244: 6049–6055
  • Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951; 193: 265–276
  • Kohtaro A., Burr I. M. Joint purification of mangano and cuprozinc superoxide dismutase from a single source. A simplified method. Analytical Biochemistry 1984; 136: 336–339
  • Salin M. L., Day E. D., Crapo J. D. Isolation and characterization of a manganese-containing superoxide dismutase from rat liver. Archives of Biochemistry and Biophysics 1978; 187: 223–228
  • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage TH. Nature 1970; 227: 680–685
  • Nishimiki M., Rao N. A., Yagi K. The occurrence of superoxide anion in the reaction of reduced phenazine merhosulfate and molecular oxygen. Biochemical and Biophysical Research Communications 1972; 46: 849–854
  • Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to polyacrylamide gels. Analytical Biochemistry 1971; 44: 276–287
  • Greenwood F. C., Hunter W. N., Glover J. S. The preparation of 131I-labelled human growth hormone of high specific radioactivity. Biochemical Journal 1963; 89: 114–123
  • Ellman G. L. Tissue sulfhydryl groups. Archives of Biochemistry and Biophysics 1959; 82: 70–77
  • Yamasaki R. B., Shimer D. A., Feeney R. E. Colorimetric determination of arginine residues in proteins by p-nitrophenylglyoxal. Analytical Biochemistry 1981; 111: 220–226
  • Tophan C. M., Dalziel K. Chemical modification of sheep-liver 6-phosphogluconate dehydrogenase by diethylpyrocarbonate. European Journal of Biochemistry 1986; 155: 87–94
  • Tuengler P., Pfletderer G. Enhanced heat, alkaline and tryptic stability of acetamidinated pig heart lactate dehydrogenase. Biochimica et Biophyska Acta 1977; 484: 1–8
  • Cutler R. G. Antioxidants and aging. American Journal of Clinical Nutrition 1991; 53: 373–379
  • Warner H. R. Superoxide dismutase, aging, and degenerative disease. Free Radical in Biology and Medicine 1994; 13: 249–258
  • II E. W., Kellog I., Fridovich I. Superoxide dismutase in the rat and mouse as a function of age and longevity. Journal of Gerontology 1976; 31: 405–408
  • Danh H., Benedetti M. S., Doster P. Differential changes in superoxide dismutase activity in brain and liver of old rats and mice. Journal of Neurochemistry 1983; 40: 1003–1007
  • Rikans L. E.C., Snowden D., Moore D. R. Effect of aging on enzymatic antioxidant defenses in rat liver mitochondria. Gerontology 1992; 38: 133–138
  • Hansford R. G. Bioenergetics in aging. Biochimica et Biophyska Acta 1983; 726: 41–80
  • Frank L., Bucher J. R., Roberts R. J. Oxygen toxicity in neonatal and adult animals of various species. Journal of Applied Physiology 1978; 45: 699–704
  • Barra D., Schinina M. E., Simmaco M., Bannister J. V., Bannister W. H., Rotilio G., Bossa F. The primary structure of human liver manganese superoxide dismutase. Journal of Biological Chemistry 1984; 259: 12595–12601
  • Parke D. V. Drug Metabolism in Man. Taylor and Francis, London 1978; 61–75
  • Ischiropoulos H., Nadziejko C. E., Kikkawa Y. Effect of aging on pulmonary superoxide dismutase. Mechanisms of Ageing and Development 1990; 52: 11–26

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