Photosynthetica 1997, 33(2):189 | DOI: 10.1023/A:1022152028173

Effects of phosphate on the activity, stability and regulatory properties of phosphoenolpyruvate carboxylase from the C4 plant Cynodon dactylon

G. Salahas1, N.A. Gavalas1
1 Department of Biology, Laboratory of Plant Physiology, University of Patras, Patras, Greece

The extraction of phosphoenolpyruvate carboxylase, PEPC (EC 4.1.1.31) from leaves of Cynodon dactylon (L.) Pers. with phosphate buffer (pH 7.4, 105 mM) was advantageous in comparison to the usual extraction with Tris-HCl buffer (pH 7.4, 100 mM); a higher activity was obtained, which was most evident at low substrate (phosphoenolpyruvate) concentrations. The PEPC activity was stable under dilution or in storage for at least 48 h at room temperature. The effects of phosphate buffer were not due to inhibition of phosphatase(s) action during the extraction, since they were also observed when the phosphates were added after the extraction with Tris-HCl. The phosphate-extracted enzyme was less responsive to both L-malate inhibition and activation by glucose-6-phosphate. The effects of phosphates might be due to preferential exclusion from the enzymic protein domain and, therefore, to a confinement of the enzyme to a fraction of the total volume.

Additional key words: glucose-6-phosphate; glycerol; L-malate; pH; phosphatase; Tris-HCl buffer

Published: March 1, 1997  Show citation

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Salahas, G., & Gavalas, N.A. (1997). Effects of phosphate on the activity, stability and regulatory properties of phosphoenolpyruvate carboxylase from the C4 plant Cynodon dactylon. Photosynthetica33(2), 189. doi: 10.1023/A:1022152028173
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