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Properties of Selenium-Induced Glutathione Peroxidase in Low-CO2-Grown Chlamydomonasreinhardtii

  • Shigeru Shigeoka
  • Toru Takeda
  • Tsuyoshi Hanaoka
  • Akiho Yokota
  • Shozaburo Kitaoka
  • Yoshitomi Iizuka

Abstract

Organisms have catalase, l-ascorbate peroxidase (AsAPOD), and glutathione peroxidase (GSHPOD) capable of scavenging H2O2, one of the toxic forms of O2. Catalase with a low affinity for H2O2 is found only in peroxisomes and cannot decompose the lipid hydroperoxides. Thus, AsA- and GSHPODs detoxify such active oxygens in energy-generating organelles. While both peroxidases have the same function in protection of the cell from oxidative damage, the distribution of the peroxidases is apparently distinct: AsAPOD occurs only in plant tissues, protozooa, and algae, while GSHPOD is only present in animal tissues (1).

Keywords

Sodium Selenite None None Cumene Hydroperoxide Immunological Property Chlamydomonas REINHARDTII 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Shigeru Shigeoka
    • 1
  • Toru Takeda
    • 1
  • Tsuyoshi Hanaoka
    • 1
  • Akiho Yokota
    • 2
  • Shozaburo Kitaoka
    • 2
  • Yoshitomi Iizuka
    • 1
  1. 1.Department of Food and NutritionKinki UniversityNara 631Japan
  2. 2.Department of Agricultural ChemistryUniversity of Osaka PrefectureSakai, Osaka 591Japan

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