Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium.

@article{BrownPeterson1995PurificationAC,
  title={Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium.},
  author={Nancy J. Brown-Peterson and Marvin L. Salin},
  journal={Journal of bacteriology},
  year={1995},
  volume={177 2},
  pages={
          378-84
        }
}
When subjected to the stress of growth in a relatively low-salt environment (1.25 M NaCl), the halophilic bacterium Halobacterium halobium induces a catalase. The protein has been purified to electrophoretic homogeneity and has an M(r) of 240,000 and a subunit size of approximately 62,000. The enzyme is active over a broad pH range of 6.5 to 10.0, with a peak in activity at pH 7.0. It has an isoelectric point of 4.0. This catalse, which is not readily reduced by dithionite, shows a Soret peak… CONTINUE READING
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