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http://dx.doi.org/10.5483/BMBRep.2015.48.2.093

Enhancement of potency and stability of human extracellular superoxide dismutase  

Kim, Sunghwan (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Kim, Hae-Young (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Kim, Jung-Ho (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Choi, Jung-Hye (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Ham, Won-Kook (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Jeon, Yoon-Jae (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Kang, Hara (Division of Life Science, College of Life Science and Bioengineering, Incheon National University)
Kim, Tae-Yoon (Department of Dermatology, College of Medicine, The Catholic University of Korea)
Publication Information
BMB Reports / v.48, no.2, 2015 , pp. 91-96 More about this Journal
Abstract
Cells express several antioxidant enzymes to scavenge reactive oxygen species (ROS) responsible for oxidative damages and various human diseases. Therefore, antioxidant enzymes are considered biomedicine candidates. Among them, extracellular superoxide dismutase (SOD3) had showed prominent efficacy against asthma and inflammation. Despite its advantages as a biomedicine, the difficulty in obtaining large quantity of active recombinant human SOD3 (rhSOD3) has limited its clinical applications. We found that a significant fraction of over-expressed rhSOD3 was composed of the inactive apo-enzyme and its potency against inflammation depended on the rate of metal incorporation. Also, purified rhSOD3 was unstable and lost its activity very quickly. Here, we suggest an ideal preparative method to express, purify, and store highly active rhSOD3. The enzymatic activity of rhSOD3 was maximized by incorporating metal ions into rhSOD3 after purification. Also, albumin or polyethylene glycol prevented rapid inactivation or degradation of rhSOD3 during preparative procedures and long-term storage.
Keywords
Extracellular superoxide dismutase; Inflammation; Metalloenzyme; Reactive oxygen species; Refolding;
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