Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: A simplified, high-yield purification of extracellular superoxide dismutase

Biochemical Journal

Volumn 317, Issue 1, 1996, Pages 51-57

  Oury, Tim D ^a   Crapo, James D ^a   Valnickova, Zuzana ^a   Enghild, Jan J ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEPARIN; HEPARIN BINDING PROTEIN; POLYMER; SUPEROXIDE DISMUTASE; TETRAMER; UREA;

ANION EXCHANGE CHROMATOGRAPHY; AORTA; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN; HUMAN TISSUE; ION EXCHANGE CHROMATOGRAPHY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; THERMOSTABILITY;

MAMMALIA;

EID: 0030014041     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3170051     Document Type: Article

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