Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.

@article{Smith1989PurificationAC,
  title={Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.},
  author={L D Smith and N Budgen and Stephen J. Bungard and M. Danson and David W. Hough},
  journal={The Biochemical journal},
  year={1989},
  volume={261 3},
  pages={973-7}
}
Glucose dehydrogenase was purified to homogeneity from the thermoacidophilic archaebacterium Thermoplasma acidophilum. The enzyme is a tetramer of polypeptide chain Mr 38,000 +/- 3000, it is catalytically active with both NAD+ and NADP+ cofactors, and it is thermostable and remarkably resistant to a variety of organic solvents. The amino acid composition was determined and compared with those of the glucose dehydrogenases from the archaebacterium Sulfolobus solfataricus and the eubacteria… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

References

Publications referenced by this paper.

Glucose dehydrogenase

  • D. C. Teller
  • J. Theor. Biol
  • 1973

Similar Papers

Loading similar papers…