Properties of Selenium-Induced Glutathione Peroxidase in Low-CO2-Grown Chlamydomonasreinhardtii
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).
KeywordsSodium Selenite None None Cumene Hydroperoxide Immunological Property Chlamydomonas REINHARDTII
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- 1.Halliwell, B. and Gutteridge, J. M. C. (1985) Free Radicals in Biology and Medicine, OxfordGoogle Scholar