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'Pulse Radiolysis' in keywords Facet   Publication Year 1979  [X]
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1979[X]
1Author    E. Lengfelder, E. F. ElstnerRequires cookie*
 Title    Cyanide Insensitive Iron Superoxide Dismutase in Euglena gracilis Comparison of the Reliabilities of Different Test Systems for Superoxide Dismutases  
 Abstract    Two proteins (Px and P2 , with mol weights of 57,500 and 27,500, respectively) were isolated from Euglena gracilis. Both proteins show cyanide-insensitive superoxide dismutase activity in the "classical" superoxide dismutase assay, using xanthine-xanthine oxidase as 0 2 ~ generator. If 0 2'~ is generated chemically (autoxidation of reduced anthraquinone), photochemically (illuminated riboflavine) or pulse radiolytically, only protein Pt but not P2 shows SOD activity. Protein P t contains l g atom (determined: 0.82) iron (no Mn or Cu) per mole protein and may thus be defined as iron-superoxide dismutase. Protein P2 , showing the spectral properties of a flavoprotein, exhibits the activities of ferredoxin-NADP-oxidoreductase and "diaphorase". The cyanide-insensi-tive SOD-activity of this "diaphorase" in the xanthine oxidase-assay for superoxide dismutase makes this classical and commonly used test unreliable for assaying cyanide insensitive SOD activities. The existence of the "prokaryote-type" of superoxide dismutase (Fe-SOD) in Euglena gracilis is exceptional for an eukaryotic, autotrophically grown organisms. 
  Reference    Z. Naturforsch. 34c, 374 (1979); received February 9 1979 
  Published    1979 
  Keywords    Fe-Superoxide Dismutase, Superoxide Dismutase Test Systems, E uglena gracilis, Pulse Radiolysis 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0374.pdf 
 Identifier    ZNC-1979-34c-0374 
 Volume    34