Metabolite regulation of partially purified soybean nodule phosphoenolpyruvate carboxylase.

@article{Schuller1990MetaboliteRO,
  title={Metabolite regulation of partially purified soybean nodule phosphoenolpyruvate carboxylase.},
  author={Kathryn A. Schuller and David H. Turpin and William C Plaxton},
  journal={Plant physiology},
  year={1990},
  volume={94 3},
  pages={
          1429-35
        }
}
Phosphoenolpyruvate carboxylase (PEPC) was purified 40-fold from soybean (Glycine max L. Merr.) nodules to a specific activity of 5.2 units per milligram per protein and an estimated purity of 28%. Native and subunit molecular masses were determined to be 440 and 100 kilodaltons, respectively, indicating that the enzyme is a homotetramer. The response of enzyme activity to phosphoenolpyruvate (PEP) concentration and to various effectors was influenced by assay pH and glycerol addition to the… CONTINUE READING
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