Purification of human copper, zinc superoxide dismutase by copper chelate affinity chromatography.
Copper, zinc superoxide dismutase was isolated from human red blood cell hemolysate by DEAE-Sepharose and copper chelate affinity chromatography. Enzyme preparations had specific activities ranging from 3400 to 3800 U/mg and recoveries were approximately 60% of the enzyme activity in the lysate. Copper chelate affinity chromatography resulted in a purification factor of about 60-fold. The homogeneity of the superoxide dismutase preparation was analyzed by sodium dodecyl sulfate-gel electrophoresis, analytical gel filtration chromatography, and isoelectric focusing.
D002614:Chelating Agents; D002846:Chromatography, Affinity / Q000379:methods; D002850:Chromatography, Gel; D003300:Copper; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007525:Isoelectric Focusing; D013482:Superoxide Dismutase / Q000097:blood / Q000302:isolation & purification*
D002614:Chelating Agents; D003300:Copper; D013482:Superoxide Dismutase