Enhancement of potency and stability of human extracellular superoxide dismutase
| Autor: | Won-Kook Ham, Hara Kang, Yoon-Jae Jeon, Hae-Young Kim, Jung-Hye Choi, Jung-Ho Kim, Sung Hwan Kim, Tae-Yoon Kim |
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| Rok vydání: | 2015 |
| Předmět: |
Antioxidant
SOD3 Recombinant Fusion Proteins Metalloenzyme medicine.medical_treatment Oxidative phosphorylation Biology Biochemistry Polyethylene Glycols law.invention law medicine Humans Potency Refolding Molecular Biology Extracellular superoxide dismutase Inflammation Reactive oxygen species chemistry.chemical_classification Protein Stability Superoxide Dismutase Albumin General Medicine Zinc HEK293 Cells Enzyme chemistry Recombinant DNA Research-Article Copper |
| Zdroj: | BMB Reports BMB REPORTS(48): 2 |
| ISSN: | 1976-6696 |
| DOI: | 10.5483/bmbrep.2015.48.2.093 |
| Popis: | 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 overexpressed 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. [BMB Reports 2015; 48(2): 91-96] |
| Databáze: | OpenAIRE |
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