Purification of pro- and eukaryotic superoxide dismutases by charge-controlled hydrophobic chromatography

The process of purifying superoxide dismutases was simplified using charge-controlled hydrophobic chromatography on 10-carboxydecyl Sepharose. In only one chromatographic step following ammonium sulphate precipitation, Fe-containing superoxide dismutase from Pseudomonas putida and Cu,Zn-containing superoxide dismutase from bovine erythrocytes were purified with an overall yield of about 70% to electrophoretic homogeneity. The specific activities of the crystalline enzyme preparations were expressed in McCord and Fridovich units and were 3000 and 3200 U/mg, respectively.