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Two proteins (P1 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 O2·− generator. If O2·− is generated chemically (autoxidation of reduced anthraquinone), photochemically (illuminated riboflavine) or pulse radiolytically, only protein P1 but not P2 shows SOD activity. Protein P1 contains 1 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-insensitive 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.

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During the incubation of soybean cotyledons with Pmg-elicitor for 22 hours the pH of the diffusion droplets increases from 7.2 to 8.3. This pH-shift is a precondition for the formation of the typical red colour of the diffusion droplet. After inhibiting the pH-shift by the use of 100 mм phosphate or Tris buffer instead of 10 mм buffer as solvent for the elicitor, the red colour is no longer formed with the exeption of 100 mM Ammediol buffer. However, the normal pattern of pterocarpan induction can be measured in the absence of the red colour in the diffusion droplet. Tris and Ammediol buffers exhibited a smaller pterocarpan induction as compared to phosphate buffer as solvent for the Pmg-elicitor.