| | 1 | Author
| E. Lengfelder, E. F. Elstner | Requires 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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| default:Reihe_C/34/ZNC-1979-34c-0374.pdf | | | | Identifier
| ZNC-1979-34c-0374 | | | | Volume
| 34 | |
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