Superoxide dismutase characterization

Beyer, W.F. and Fridovich, I. (1989). Characterization of a superoxide dismutase mimic prepared from desferrioxamine and MnOa. Arch. Biochem. Biophys. 271, 149-156. 

M.L. Salin and W.W. Wilson, Porcine superoxide dismutase. Isolation and characterization of a relatively basic cuprozinc enzyme. Molec. Cell Biochem. 36, 157-161 (1981). 

SOD in Figure 5 demonstrates the effect of superoxide dismutase on PCL. Its effect is characterized by an inhibition of the chemiluminescence intensity without having an impact on the lag phase. According to McCord and Frido-vich [27] (50% test signal inhibition), 1 activity unit in this system refers to approximately 100 ng of the enzyme preparation of the Sigma Co. 

Dos Santos WG, Pacheco I, Liu MY, et al. 2000. Purification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas. J Bacteriol 182 796-804. 

Lehmann Y, Meile L, Teuber M. 1996. Rubrerythrin from Clostridium perfringens cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function. J Bacteriol 178 7152-8. 

Isolation, Purification, Characterization, and Assay of Antioxy-genic Enzymes Isolation and characterization of superoxide dis-mutase, 105, 88 superoxide dismutase assays, 105, 93 assays of glutathione peroxidase, 105, 114 catalase in vitro, 105, 121 assays of lipoxygenase, 105, 126. 

Calabrese, L. et al. Preparation and preliminary characterization of hybrids of bovine Cu, Zn superoxide dismutase with selectively metal-free and metal-substituted subunits. In Chemical and Biochemical Aspects of Superoxide and Superoxide Dismutase (Bannister, J. V., Hill, H. A. O., eds.). New York-Amsterdam-Oxford, Elsevier/North-Holland, 1980, pp. 265-271... 

Three Mn catalases have been purified and characterized, and all appear to have similar Mn structures (17). The Mn stoichiometry is ca. 2 Mn/subunit, suggesting a dinuclear Mn site. The optical spectrum of the as-isolated enzyme has a broad weak absorption band at ca. 450-550 nm in addition to the protein absorption at higher energies. This spectrum is similar to those observed for Mn(III) superoxide dismutase and for a variety of Mn(III) model complexes, thus implying that at least some of the Mn in Mn catalase is present as Mn(III). In particular, the absorption maximum at ca. 500 nm is similar in energy and intensity to the transitions seen for oxo-carboxylato-bridged Mn dimers, suggesting that a similar core structure may be seen for Mn catalase (18). 

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