Superoxide Dismutase Modification and Genotoxicity of Transition-Metal Ion Chelators

  • T. P. Coogan
  • D. G. Stump
  • D. A. Barsotti
  • I. Y. Rosenblum
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 197)


Superoxide radicals are considered to be of major significance in the mechanism of oxygen-mediated cell toxicity. Superoxide and/or uperoxide-derived free radical species have been implicated in damage to cells in vivo (Fridovich, 1978) and in vitro (Holland et al., 1982). Specifically, damage to DNA (Emerit et al., 1982; Cunningham and Lokesh, 1983) proteins (Lavelle et al., 1973) and lipids (Chance et al., 1979) has been reported in a number of experimental systems. Superoxide dismutase (SOD), a widely distributed enzyme in aerobic tissues, is recognized for its important scavenging function in the primary defense of cells (Fridovich, 1978). SOD protects the cell against the deleterious effects of superoxide by catalyzing its dismutation to molecular oxygen and hydrogen peroxide. In eucaryotic cells, two forms of SOD are found; a cytoplasmic enzyme containing copper and zinc and a mitochondrial enzyme containing manganese (Fridovich, 1978). The importance of the metalloprotein complex in the catalytic function of SOD has been firmly established (Fridovich, 1978).


Male Germ Cell Spermatogenic Cell Alkaline Elution Tetrapropylammonium Hydroxide Potassium Superoxide 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • T. P. Coogan
    • 1
  • D. G. Stump
    • 1
  • D. A. Barsotti
    • 1
  • I. Y. Rosenblum
    • 1
  1. 1.Department of Pharmacology and ToxicologyPhiladelphia College of Pharmacy and SciencePhiladelphiaUSA

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