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RADIATION PROTECTION BY SUPEROXIDE DISMUTASE
Photochemistry and Photobiology, 1978Abstract— Protection of X‐irradiated mice by bovine superoxide dismutase is enhanced when the enzyme is given intravenously both before and after the exposure. With the combined treatment, the LD50(30) dose is increased from 734 ± 8 to 1144 ± 15rad for a dose reduction factor of 1.56 ± 0.04.
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Superoxide dismutase: improved assays and an assay applicable to acrylamide gels.
Analytical Biochemistry, 1971C. Beauchamp, I. Fridovich
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Lactoperoxidase, a dithionite ion dismutase
European Journal of Biochemistry, 1984The dithionite ion is catalytically disproportionated by lactoperoxidase with Km= 0.36 mM in 100 mM glycine HCl pH 3.0. The products formed are thiosulfate and hydrogensulfite ions. The rate of reaction is considerably increased at low pH with a pKa at 3–3.5 possibly indicating the involvement of a carboxyl group.
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Analysis of Superoxide Dismutase Activity
Current Protocols in Toxicology, 1999AbstractMeasuring the activity of superoxide dismutases (SODs), the enzymes responsible for maintaining the steady state level of hydrogen peroxide, is challenging because the substrate is unstable at physiological pH and it reacts with itself. Fortunately the rate of reaction with dismutase is far greater than the rate of self reaction.
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Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions.
Analytical Biochemistry, 1987W. Beyer, I. Fridovich
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