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

Journal Article · Thu May 15 00:00:00 EDT 1986 · Anal. Biochem.; (United States)

DOI:https://doi.org/10.1016/0003-2697(86)90246-0· OSTI ID:5457923

Weslake, R J; Chesney, S L; Petkau, A; Friesen, A D

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.

• Research Organization: Univ. of Manitoba, Winnipeg
• OSTI ID: 5457923
• Journal Information: Anal. Biochem.; (United States), Vol. 155:1
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC
ORGANIC
PHYSICAL AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
SUPEROXIDE DISMUTASE
PURIFICATION
CHELATES
CHROMATOGRAPHY
COPPER
ELECTROPHORESIS
ENZYME ACTIVITY
ERYTHROCYTES
HEMOLYSIS
ZINC
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
COMPLEXES
ELEMENTS
ENZYMES
LYSIS
MATERIALS
METALS
OXIDOREDUCTASES
PATHOLOGICAL CHANGES
SEPARATION PROCESSES
TRANSITION ELEMENTS
400102* - Chemical & Spectral Procedures
550200 - Biochemistry