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. 2008 Dec 4;43(1):4–12. doi: 10.1080/10715760802582183

Figure 2.

Figure 2

Superoxide dismutase activity of MitoTEMPOL. Superoxide was produced by mixing 20 mU xanthine oxidase with 10 mM acetaldehyde in 50 mM potassium phosphate buffer (pH 8) supplemented with 500 μg/ml ferricytochrome c at 37°C. The rate of cytochrome c reduction was followed at 550 nm for 60 s after which the appropriate amount of SOD, MitoTEMPOL, TEMPOL or propylTPP was added and the rate was followed for another 60 s. The slope of the cytochrome c reduction progress curve was measured after each addition and is expressed as a percentage of the slope before the addition. Results are means ± SD of three measurements. ** p < 0.01; § p < 0.05 with respect to the same concentration of MitoTEMPOL.