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), Journal Name: Anal. Biochem.; (United States) Vol. 155:1; ISSN ANBCA
• Country of Publication: United States
• Language: English

Related Subjects

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