✦ LIBER ✦

Purification of human copper, zinc superoxide dismutase by copper chelate affinity chromatography

✍ Scribed by Randall J. Weselake; Sharon L. Chesney; Abram Petkau; Albert D. Friesen

Publisher: Elsevier Science
Year: 1986
Tongue: English
Weight: 848 KB
Volume: 155
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(86)90246-0

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✦ Synopsis

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.

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