Sulfate Ion Effect on Stability and Regulatory Properties of PEP Carboxylase from the C4Plant Cynodon dactylon |
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Authors: | Salahas G. Angelopoulos K. Zervoudakis G. Georgiou C. D. |
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Affiliation: | (1) Department of Biology, Laboratory of Plant Physiology, University of Patras, Patra, 26100, Greece |
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Abstract: | When Tris–SO4was used as an extraction buffer for phosphoenolpyruvate carboxylase (PEPC) from leaves of the C4plant Cynodon dactylon(L.) Pers., a higher extractable activity was obtained as compared to Tris–HCl, especially at low phosphoenolpyruvate concentrations and an assay pH of 7.2. The Tris–SO4-extracted PEPC activity was stable under dilution and remained unchanged for at least 24 h at 22°C. This enzyme was less sensitive to both activation by glucose-6-phosphate and inhibition by L-malate. The effects of Tris–SO4could be attributed to its preferential exclusion from the enzymic protein domain and, therefore, to a shifting of this oligomeric enzyme to a more aggregable form that is more stable and active. |
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Keywords: | Cynodon dactylon phosphoenolpyruvate carboxylase enzyme activation glucose-6-phosphate malate |
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