Cloning, expression, purification and activation by Na ion of halophilic alkaline phosphatase from moderate halophile Halomonas sp. 593.

@article{Ishibashi2011CloningEP,
  title={Cloning, expression, purification and activation by Na ion of halophilic alkaline phosphatase from moderate halophile Halomonas sp. 593.},
  author={Matsujiro Ishibashi and Kazuki Oda and Tsutomu Arakawa and Masao Tokunaga},
  journal={Protein expression and purification},
  year={2011},
  volume={76 1},
  pages={
          97-102
        }
}
We have succeeded in the cloning of alkaline phosphatase gene, haalp, from moderate halophile Halomonas sp. 593. A deduced amino acid sequence showed a high ratio of acidic to basic amino acids, characteristic of halophilic proteins. The gene product was efficiently expressed in Escherichia coli BL21 Star (DE3) pLysS, but in an inactive form. The purified recombinant HaALP was separated into four fractions by gel filtration. When they were dialyzed against 50 mM Tris-HCl (pH 8.0)/2 mM MgCl… CONTINUE READING

References

Publications referenced by this paper.
SHOWING 1-10 OF 33 REFERENCES

B

  • R. Helland, R. L. Larsen
  • Asgeirsson, The 1.4 Å crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase, Biochim. Biophys. Acta 1794
  • 2009
VIEW 6 EXCERPTS
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