Purification and Partial Kinetic and Physical Characterization of Two Chloroplast-Localized NADP-Specific Glutamate Dehydrogenase Isoenzymes and Their Preferential Accumulation in Chlorella sorokiniana Cells Cultured at Low or High Ammonium Levels.

@article{Bascomb1987PurificationAP,
  title={Purification and Partial Kinetic and Physical Characterization of Two Chloroplast-Localized NADP-Specific Glutamate Dehydrogenase Isoenzymes and Their Preferential Accumulation in Chlorella sorokiniana Cells Cultured at Low or High Ammonium Levels.},
  author={N F Bascomb and Richard R Schmidt},
  journal={Plant physiology},
  year={1987},
  volume={83 1},
  pages={75-84}
}
Two ammonium-inducible, chloroplast-localized NADP-specific glutamate dehydrogenase isoenzymes were purified to homogeneity from Chlorella sorokiniana. These isoenzymes were homopolymers of either alpha- or beta-subunits with molecular weights of 55,500 or 53,000, respectively. The alpha-isoenzyme was preferentially induced at low ammonium concentrations (2 millimolar or lower), whereas only the beta-isoenzyme accumulated after cells were fully induced (120 minutes) at high ammonium… CONTINUE READING

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Evidence for the participation of NADP-glutamate dehydrogenase in the ammonium assimilation of Chlorella sorokiniana

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1 Excerpt

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