An inter-subunit disulfide bond affects affinity of human lung extracellular superoxide dismutase to heparin

Free Radical Research

Volumn 37, Issue 8, 2003, Pages 823-827

  Ookawara, Tomomi ^a   Eguchi, Hironobu ^a   Kizaki, Takako ^b   Nakao, Chitose ^c   Sato, Yuzo ^c   Imazeki, Nobuo ^d   Matsubara, Osamu ^d   Ohno, Hideki ^b   Suzuki, Keiichiro ^a  

^a HYOGO COLLEGE OF MEDICINE   (Japan)

^b KYORIN UNIVERSITY   (Japan)

^c NAGOYA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^d NATIONAL DEFENSE MEDICAL COLLEGE   (Japan)

Author keywords

Affinity for heparin; Disulfide bond; EC SOD; Human; Purification

Indexed keywords

ENZYME ANTIBODY; HEPARIN; SUPEROXIDE DISMUTASE;

AFFINITY CHROMATOGRAPHY; ANTIBODY SPECIFICITY; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; COLUMN CHROMATOGRAPHY; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME PURIFICATION; HUMAN; HUMAN TISSUE; LUNG PARENCHYMA; OXIDATION REDUCTION STATE; PROTEIN LOCALIZATION; REGULATORY MECHANISM; REVIEW; TISSUE HOMOGENATE; WESTERN BLOTTING;

BLOTTING, WESTERN; CERAMICS; CHROMATOGRAPHY; CHROMATOGRAPHY, AFFINITY; DISULFIDES; DURAPATITE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HEPARIN; HUMANS; LUNG; OXIDATION-REDUCTION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEPHAROSE; SODIUM CHLORIDE; SUPEROXIDE DISMUTASE;

EID: 0041695220     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/1071576031000119404     Document Type: Review

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