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Pacquit V, Giglioli N, Crétin C, et al. Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase from Sorghum: An immunological study using specific anti-phosphorylation site-antibodies. Photosynth Res. 1995;43(3):283-8doi: 10.1007/BF00029941.
Pacquit, V., Giglioli, N., Crétin, C., Pierre, J. N., Vidal, J., & Echevarria, C. (1995). Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase from Sorghum: An immunological study using specific anti-phosphorylation site-antibodies. Photosynthesis research, 43(3), 283-8. https://doi.org/10.1007/BF00029941
Pacquit, V, et al. "Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase from Sorghum: An immunological study using specific anti-phosphorylation site-antibodies." Photosynthesis research vol. 43,3 (1995): 283-8. doi: https://doi.org/10.1007/BF00029941
Pacquit V, Giglioli N, Crétin C, Pierre JN, Vidal J, Echevarria C. Regulatory phosphorylation of C4 phosphoenolpyruvate carboxylase from Sorghum: An immunological study using specific anti-phosphorylation site-antibodies. Photosynth Res. 1995 Mar;43(3):283-8. doi: 10.1007/BF00029941. PMID: 24306851.
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Photosynth Res. 1995 Mar;43(3):283-8. doi: 10.1007/BF00029941.

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

Photosynthesis research

V Pacquit, N Giglioli, C Crétin, J N Pierre, J Vidal, C Echevarria

Affiliations

  1. Institut de Biotechnologie des Plantes, UA CNRS D1128, Université de Paris-Sud, 91405, Orsay Cedex, France.

PMID: 24306851 DOI: 10.1007/BF00029941

Abstract

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 its functional and regulatory properties that mimicked phosphorylation of Ser-8. A series of recombinant C4 PEPCs mutated in the N-terminal phosphorylation domain and a C3-like PEPC isozyme from Sorghum behaved similarly to their C4 counterpart with respect to these phosphorylation-site antibodies.

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