Further thermal characterization of an aspartate aminotransferase from a halophilic organism.

@article{Muriana1994FurtherTC,
  title={Further thermal characterization of an aspartate aminotransferase from a halophilic organism.},
  author={Francisco Jos{\'e} Muriana and M C Alvarez-Ossorio and A. M. Relimpio},
  journal={The Biochemical journal},
  year={1994},
  volume={298 ( Pt 2)},
  pages={465-70}
}
Aspartate aminotransferase (AspAT, EC 2.6.1.1) from the halophilic archaebacterium Haloferax mediterranei was purified [Muriana, Alvarez-Ossorio and Relimpio (1991) Biochem. J. 278, 149-154] and further characterization of the effects of temperature on the activity and stability of the halophilic AspAT were carried out. The halophilic transaminase is most active at 65 degrees C and stable at high temperatures, under physiological or nearly physiological conditions (3.5 M KCl, pH 7.8). Thermal… CONTINUE READING