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Activity of glutamate dehydrogenase is increased in ammonia-stressed hybridoma cells

✍ Scribed by Hendrik P. J. Bonarius; José H. M. Houtman; Cornelis D. de Gooijer; Johannes Tramper; Georg Schmid

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
81 KB
Volume
57
Category
Article
ISSN
0006-3592

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✦ Synopsis

The effect of added ammonia on the intracellular fluxes in hybridoma cells was investigated by metabolic-flux balancing techniques. It was found that, in ammonia-stressed hybridoma cells, the glutamatedehydrogenase flux is in the reverse direction compared to control cells. This demonstrates that hybridoma cells are able to prevent the accumulation of ammonia by converting ammonia and ␣-ketoglutarate into glutamate. The additional glutamate that is produced by this flux, as compared to the control culture, is converted by the reactions catalyzed by alanine aminotransferase (45% of the extra glutamate) and aspartate aminotransferase (37%), and a small amount is used for the biosynthesis of proline (6%). The remaining 12% of the extra glutamate is secreted into the culture medium. The data suggest that glutamate dehydrogenase is a potential target for metabolic engineering to prevent ammonia accumulation in high-cell-density culture.

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