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.
Grunow
M
M
Bereich Biochemie der Sektion Biowissenschaften, Universität Leipzig, Germany.
Schöpp
W
W
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D016958:Pseudomonas putida / Q000201:enzymology*; D013482:Superoxide Dismutase / Q000302:isolation & purification*
D013482:Superoxide Dismutase