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Quantitative Immunochemistry of Plant Phosphoenolpyruvate Carboxylases

  • J. Brulfert
  • J. Vidal
Part of the Modern Methods of Plant Analysis book series (MOLMETHPLANT, volume 4)

Abstract

Since its discovery (Bandurski and Greiner 1953) phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) has attracted increasing interest among plant scientists. The enzyme catalyses the reaction of CO3H and phosphoenolpyruvate to produce oxaloacetate, immediately reduced to form malate; this latter can be oxidatively decarboxylated by NADP malic enzyme, and thus, appears to be a physiological vector for carbon (CO2) and energy (reducing power). Extensive studies established the ubiquitous presence of PEPC in plants and its functional, regulatory and physico-chemical properties have been described by several groups. PEPC appears to be involved in number of physiological roles, wich were recently extensively reviewed [Physiol Vég 21:5 (1983)]. More particularly PEPC seems to play a fundamental role in adaptation of plant organisms to changes in physiological and environmental parameters; for this reason PEPC can be considered as a good marker for differentiation of physiological processes and for operation of adaptive metabolic pathways. In some cases isoforms involved in specific physiological roles, were described as typical.

Keywords

Crassulacean Acid Metabolism Pyruvate Carboxylase Phosphoenolpyruvate Carboxylase Immune Serum Cyanogen Bromide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Bandurski RS, Greiner CM (1953) The enzymatic synthesis of oxalacetate from phosphoryl-enolpyruvate and carbon dioxide. J Biol Chem 204: 781–786PubMedGoogle Scholar
  2. Brulfert J, Queiroz O (1982) Photoperiodism and Crassulacean acid metabolism III. Different characteristics of the photoperiod-sensitive and non-sensitive isoforms of phosphoenolpyrúvate carboxylase and Crassulacean acid metabolism operation. Planta (Berl) 154: 339–343CrossRefGoogle Scholar
  3. Brulfert J, Guerrier D, Queiroz O (1982a) Photoperiodism and Crassulacean acid metabolism II Relations between leaf ageing and photoperiod in Crassulacean acid metabolism induction. Planta (Berl) 154: 332–338CrossRefGoogle Scholar
  4. Brulfert J, Müller D, Kluge M, Queiroz O (1982b) Photoperiodism and Crassulacean acid metablism I Immunological and kinetic evidences for different patterns of phosphoenolpyru`vate carboxylase isoforms in photoperiodically inducible and non-inducible Crassulacean acid metabolism plants. Planta (Berl) 154: 326–331CrossRefGoogle Scholar
  5. Brulfert J,. Vidal J, Gadal P, Queiroz O (1982c) Daily rhythm of phospoenolpyruvate carboxylase in Crassulacean acid metabolism plants. Immunological evidence for the absence of a rhythm in protein synthesis. Planta (Berl) 156: 92–94CrossRefGoogle Scholar
  6. Crétin C, Perrot-Rechenmann C, Vidal J, Gadal P, Loubinoux B, Tabach S (1983) Study on plant phosphoenolpyruvate carboxylase: sensitivity to herbicides and immunochemical reactivity. Physiol Veg 21: 927–933Google Scholar
  7. Crétin C, Vidal J, Suzuki A, Gadal P (1984) Isolation of plant phosphoenolpyruvate carboxylase by high-performance size-exclusion chromatography. J Chromatogr 315: 430–434CrossRefGoogle Scholar
  8. Harpster MH, Taylor WC (1986) Differential expression of the maize PEPC gene family. J Biol Chem 261: 6132–6136PubMedGoogle Scholar
  9. Hatch MD, Oliver JB (1978) Activation and inactivation of phosphoenolpyruvate carboxylase in leaf extract from C4 species. Aust J Plant Physiol 5: 571–580CrossRefGoogle Scholar
  10. Hayakawa S, Matsunaga K, Sugiyama T (1981) Light induction of phosphoenolpyruvate carboxylase in etiolated Maize leaf tissue. Plant Physiol (Bethesda) 67: 133–138CrossRefGoogle Scholar
  11. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bac-teriophage T4. Nature 227: 680–685PubMedCrossRefGoogle Scholar
  12. Laurell CB (1966) Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 15: 45–52PubMedCrossRefGoogle Scholar
  13. Mancini G, Carbonara AO, Heremans SJF (1965) Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry 2: 235–254PubMedCrossRefGoogle Scholar
  14. Manetas Y (1982) Changes in properties of phosphoenolpyruvate carboxylase from the CAM plant Sedum praealtum DC. upon dark/light transition and their stabilization by glycerol. Photosynth Res 7: 321–333CrossRefGoogle Scholar
  15. Miginiac-Maslow M, Vidal J, Bismuth E, Hoarau A, Champigny ML (1983) Effets de la carence et la réalimentation en phosphate sur l’équilibre énergétique et l’activité phosphoenolpyruvate carboxylase de jeunes plantes de Blé. Physiol Vég 21: 325–335Google Scholar
  16. Müller D, Kluge M, Gröschel-Stewart U (1982) Comparative studies in immunological and molecular properties of phosphoenolpyruvate carboxylase in species of Sedum and Kalanchoe performing crassulacean acid metabolism ( CAM ). Plant Cell Environ 5: 223–230Google Scholar
  17. Nato A, Vidal J (1983) Phosphoenolpyruvate carboxylase activity in relation to physiological processes during the growth of cell suspension cultures from Nicotiana tabacum. Physiol Veg 21: 1031–1039Google Scholar
  18. Ouchterlony H (1958) Diffusion in gel methods for immunological analysis. Prog Allergy 5: 1–78PubMedGoogle Scholar
  19. Perrot C, Vidal J, Burlet A, Gadal P (1981) On the cellular localization of phosphoenolpyruvate carboxylase. Planta (Berl) 151: 226–231CrossRefGoogle Scholar
  20. Perrot-Rechenmann C, Vidal J, Brulfert J, Burlet A, Gadal P (1982) A comparative immunocytochemical localization study of phosphoenolpyruvate carboxylase in leaves of higher plants. Planta (Berl) 155: 24–30CrossRefGoogle Scholar
  21. Robertson A, Kerr HW (1971) Properties of PEPC isolated from Maize leaves. Biochem J 125: 34Google Scholar
  22. Uedan K, Sugiyama T (1976) Purification and characterization of phosphoenolpyruvate carboxylase from maize leaves. Plant Physiol (Bethesda) 57: 906–910CrossRefGoogle Scholar
  23. Vidal J, Gadal P (1983) Influence of light on phosphoenolpyruvate carboxylase in sorghum leaves I. Identification and properties of two isoforms. Physiol Plant 57: 119–123CrossRefGoogle Scholar
  24. Vidal J, Cavalié G, Gadal P (1976) Etude de la phosphoenolpyruvate carboxylase du haricot et du sorgho par électrophorèse sur gel de polyacrylamide. Plant Sci Lett 7: 265–270CrossRefGoogle Scholar
  25. Vidal J, Godbillon G, Gadal P (1980) Recovery of active, highly purified phosphoenol-pyruvate carboxylase from specific immunoadsorbent column FEBS Lett 118: 31–34Google Scholar
  26. Vidal J, Crétin C, Gadal P (1983a) The mechanism of photocontrol of phosphoenolpyru-vate carboxylase in sorghum leaves. Physiol Vég 21: 977–986Google Scholar
  27. Vidal J, Godbillon G, Gadal P (1983b) Influence of light on phosphoenolpyruvate carboxylase in sorghum leaves II. Immunochemical study. Physiol Plant 57: 124–128CrossRefGoogle Scholar
  28. Vidal J, Nguyen J, Perrot-Rechenmann C, Gadal P (1986) De novo synthesis of phosphoenolpyruvate carboxylase during development of soybean root nodules. Planta 167: 190–195CrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • J. Brulfert
  • J. Vidal

There are no affiliations available

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