Superoxide Dismutase Enhances the Toxicity of 3-Hydroxyanthranilic Acid to Bacteria

References

• Bannister J. V., Bannister W. H., Rotilio G. Aspects of the structure, function and applications of superoxide dismutase. CRC Critical Reviews in Biochemistry 1987; 22: 111–180
   PubMed Web of Science ®Google Scholar
• Zimmerman R., Cerutti P. Active oxygen acts as a promoter of transformation in mouse embryo C3H/10T1/2/C18 fibroblasts. Proceedings of the National Academy of Science of the United States of America 1984; 81: 2085–2087
   PubMed Web of Science ®Google Scholar
• Oberley L. W., Buettner G. R. Role of superoxide dismutase in cancer: a review. Cancer Research 1979; 39: 1141–1149
   PubMed Web of Science ®Google Scholar
• Leibovitz B. E., Siegel B. V. Aspects of free radical reactions in biological systems; aging. Journal of Gerontology 1980; 35: 45–56
   PubMed Web of Science ®Google Scholar
• Babior B. M., Kipnes R. S., Curnutte J. T. Biological defence mechanisms; the production by leukocytes of superoxide, a potential bactericidal agent. Journal of Clinical Investigation 1973; 52: 741–744
   PubMed Web of Science ®Google Scholar
• Allen R. C., Yevich S. J., Orth R. W., Steele R. H. The superoxide anion and singlet molecular oxygen; their role in the microbicidal activity of the polymorphponuclear leucocyte. Biochemical and Biophysical Research Communications 1974; 60: 909–917
   PubMedGoogle Scholar
• Hassan N. M., Fridovich I. Regulation of the synthesis of superoxide dismutase in. Escherichia coli. Journal of Biological Chemistry 1977; 252: 7667–7672
   PubMed Web of Science ®Google Scholar
• Natvig D. O., Imlay K., Touati D., Hallewell R. A. Human copper-zinc superoxide dis mutase complements superoxide dismutase-deficient. Escherichia coli mutants. Journal of Biological Chemistry 1987; 262: 14697–14701
   PubMed Web of Science ®Google Scholar
• Lown J. W., Sim S.-K., Majumdar K. C., Chang R.-Y. Strand scission of DNA by bound adriamycin and daunorubicin in the presence of reducing agents. Biochemical and Biophysical Re- search Communications 1977; 76: 705–710
   PubMed Web of Science ®Google Scholar
• Grankvist K., Marklund S., Sehlin J., Taljedal I.-B. Superoxide dismutase, catalase and scavengers of hydroxyl radical protect against the toxic action of alloxan on pancreatic islet cells. in vitro. Biochemical Journal 1979; 182: 17–25
   PubMed Web of Science ®Google Scholar
• Fischer L. J., Hamburger S. A. Inhibition of alloxan action in isolated pancreatic islets by superoxide dismutase, catalase, and a metal chelator. Diabetes 1980; 29: 213–216
   PubMed Web of Science ®Google Scholar
• Scott M. D., Meshnick S. R., Eaton J. W. Superoxide dismutase-rich bacteria. Journal of Biological Chemistry 1987; 262: 3640–3645
   PubMed Web of Science ®Google Scholar
• Boyland E., Williams D. C. The metabolism of tryptophan. Biochemical Journal 1956; 64: 578–582
   PubMed Web of Science ®Google Scholar
• Boyland E., Watson G. 3-Hydroxyanthranilic acid, a carcinogen produced by endogenous metabolism. Nature 1956; 177: 837–838
   PubMed Web of Science ®Google Scholar
• Allen M. J., Boyland E., Dukes C. E., Horning E. S., Watson J. G. Cancer of the urinary bladder induced in mice with metabolites or aromatic amines and tryptophan. British Journal of Cancer 1957; 11: 212–228
   PubMed Web of Science ®Google Scholar
• Bryan G. T., Brown R. R., Price J. M. Mouse bladder carcinogenicity of certain tryptophan metabolites and other aromatic nitrogen compounds suspended in cholesterol. Cancer Research 1964; 24: 596–602
   PubMed Web of Science ®Google Scholar
• Ehrensvard G., Liljekvist J., Health R. G. Oxidation of 3-hydroxy-anthranilic acid by human serum. Acta Chemica Scandinavica 1960; 14: 2081–2088
   Google Scholar
• Subba Rao P. V., Vaidyanathan C. S. Enzymic conversion of 3-hydroxyanthranilic acid into cinnabarinic acid. Biochemical Journal 1966; 99: 317–322
   Google Scholar
• Ogawa H., Nagamura Y., Ishiguro I. Cinnabarinate formation in malpighian tubules of the silkwork, Bombxy mori reaction mechanism of cinnabarinate formation in the presence of catalase and manganes ions. Hoppe-Seyler's Zeitschrifl für Physiologische Chemie 1983; 364: 1507–1518
   Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase. Journal of Biological Chemistry 1969; 244: 6049–6055
   PubMed Web of Science ®Google Scholar
• Blech D. M., Borders C. L., Jr. Hydroperoxide anion, HO2−, is an affinity reagent for the inactivation of yeast Cu, Zn superoxide dismutase: modification of one histidine per subunit. Archives of Biochemistry and Biophysics 1983; 224: 579–586
   PubMedGoogle Scholar
• 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: 265–275
   PubMed Web of Science ®Google Scholar
• Beers R. F., Jr., Sizer I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. Journal of Biological Chemistry 1952; 195: 133–140
   PubMed Web of Science ®Google Scholar
• Levin D. E., Hollstein M., Christman M. F., Schwiers E. A., Ames B. N. A new Salmonella tester strain (TA102) wit A-T base pairs at the site of mutation detects oxidative mutagens. Proceedings of the National Academy of Science of the United States of America 1982; 79: 7445–7449
   PubMed Web of Science ®Google Scholar
• Dykens J. A., Sullivan S. G., Stern A. Oxidative reactivity of the tryptophan metabolites 3-hydroxyanthranilate, cinnabarinate, quinolinate and picolinate. Biochemical Pharmacology 1987; 36: 211–217
   PubMed Web of Science ®Google Scholar
• Iwahashi H., Ishii T., Sugata R., Kido R. Superoxide dismutase enhances the formation of hydroxyl radicals in the reaction of 3-hydroxyanthranilic acid with molecular oxygen. Biochemical Journal 1988; 251: 893–899
   PubMed Web of Science ®Google Scholar
• Ishii T., Iwahashi H., Sugata R., Kido R., Fridovich I. Superoxide dismutases enhance the rate of autoxidation of 3-hydroxyanthranilic acid. Archives of Biochemistry and Biophysics 1990; 276: 248–250
   Google Scholar
• Miller T. E. Killing and lysis of gram-negative bacteria through the synergestic effect of hydrogen peroxide, ascorbic acid, and lysozyme. Journal of Bacteriology 1969; 98: 949–955
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M.C., Richmond R., Halliwell B. Inhibition of the iron-catalyzed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine. Biochemical Journal 1979; 184: 469–472
   PubMed Web of Science ®Google Scholar