Abstract
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.
