Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase from Sorghum: An immunological study using specific anti-phosphorylation site-antibodies

@article{Pacquit1995RegulatoryPO,
  title={Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase from Sorghum: An immunological study using specific anti-phosphorylation site-antibodies},
  author={Val{\'e}rie Pacquit and N. Giglioli and Claude Cr{\'e}tin and Jean Noel Pierre and Jean Vidal and Cristina Echevarr{\'i}a},
  journal={Photosynthesis Research},
  year={1995},
  volume={43},
  pages={283-288}
}
A peptide containing the N-terminal phosphorylation site (Ser-8) of Sorghum C4-phospho enolpyruvate carboxylase (PEPC) was synthesized, purified and used to raise an antiserum in rabbits. Affinity-purified IgGs prevented PEPC phosphorylation in a reconstituted in vitro assay and reacted with both the phosphorylated and dephosphorylated forms of either native or denatured PEPC in immunoblotting experiments. Saturation of dephospho-PEPC with these specific IgGs resulted in a marked alteration of… CONTINUE READING

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