• Corpus ID: 21277605

[Purification and properties of glutamate dehydrogenase from Pseudomonas pseudoalcaligenes].

@article{Ding1999PurificationAP,
  title={[Purification and properties of glutamate dehydrogenase from Pseudomonas pseudoalcaligenes].},
  author={S Ding and Z. Yang and Y. Tang and Rongrong Jing and Shaojun Liu},
  journal={Wei sheng wu xue bao = Acta microbiologica Sinica},
  year={1999},
  volume={39 5},
  pages={
          475-7
        }
}
  • S. Ding, Z. Yang, +2 authors S. Liu
  • Published 1 October 1999
  • Chemistry, Medicine
  • Wei sheng wu xue bao = Acta microbiologica Sinica
Glutamate dehydrogenase was purified from the crude extract of Pseudomonas pseudoal-caligenes. The enzyme had a molecular weight of 290,000 and was composed of six subunits with identical molecular weight of 47,000. The enzyme was highly specific for NADP(H) and the substrates. The biochemical properties such as kinetic parameters and heat stability were also examined. The purified GDH showed considerable loss of activity upon freezing.