Molecular Cloning, Expression and Functional Characterization of a Peroxiredoxin from the Mole Cricket, Gryllotalpa orientalis

  • Kim, Iksoo (Department of Sericulture and Entomology, Natinal of Agricultural Science and Technology) ;
  • Kang sun Ryu (Department of Sericulture and Entomology, Natinal of Agricultural Science and Technolog) ;
  • Kim, Jin-Won (Department of Sericulture and Entomology, Natinal of Agricultural Science and Technolog) ;
  • Ahn, Mi-Young (Department of Sericulture and Entomology, Natinal of Agricultural Science and Technolog) ;
  • Kwang Sik (College of Natural Resources and Life Sciences, Dong-A University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Sciences, Dong-A University)
  • Published : 2003.10.01

Abstract

Peroxiredoxins are a family of antioxidant proteins ubiquitously found in all living organisms. A type of peroxidase enzyme, named thioredoxin peroxidase (TPx), that reduces $H_2O$$_2$ with the use of electrons from thioredoxin and contains two essential cysteines was identified in a wide variety of organisms ranging from prokaryotes to mammals. TPx homologs, termed peroxiredoxin (Prx), have also been identified and include several proteins, designated 1-Cys Prx, that contain only one conserved cysteine. (omitted)

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