Abstract
On the basis of the thermal stability of erythrocuprein (Cu2Zn2-superoxide dismutase) a rapid preparation technique was devised and successfully employed to isolate this protein. Partial heat-deterioration of the haemolysate and subsequent chromatography of the supernatant on DEAE-Sephacel and Sephadex G-75 yielded an electrophoretically homogeneous protein within a few days. The physicochemical properties and biochemical function were identical with those reported for Cu2Zn2-superoxide dismutases prepared by established methods.
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Selected References
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