極限環境生物学会誌
Online ISSN : 2186-9936
Purification of thermophilic superoxide dismutase by utilizing the surfactant
Ding LYWatanabe KYasui M
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ジャーナル オープンアクセス

2014 年 13 巻 2 号 p. 53-58

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抄録
Superoxide dismutase (SOD) is an enzyme that alternately catalyzes the dismutation of anion radicals in living cells. Manganese type SOD (MnSOD) has been purified and partially characterized from the thermophilic bacteria; Bacillus stearothermophilus strain C36. The purification was achieved using a column chromatography on Sephacryl S-200 in the presence of lauryl dodecyl sulfate (SDS). SDS was used to separate MnSOD from other proteins. The final recovery rate was 33 %. This recovery rate was much higher than other authentic methods (1.6 % – 13.6 %). This SDS-containing gel chromatography was available for the purification of a protein from the other thermophile.
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© 2014 Japanese Society for Extremophiles
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