Sulfate Ion Effect on Stability and Regulatory Properties of PEP Carboxylase from the C4Plant Cynodon dactylon

Sulfate Ion Effect on Stability and Regulatory Properties of PEP Carboxylase from the C4Plant... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Plant Physiology Springer Journals

Sulfate Ion Effect on Stability and Regulatory Properties of PEP Carboxylase from the C4Plant Cynodon dactylon

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Publisher
Kluwer Academic Publishers-Plenum Publishers
Copyright
Copyright © 2001 by MAIK “Nauka/Interperiodica”
Subject
Life Sciences; Plant Sciences
ISSN
1021-4437
eISSN
1608-3407
D.O.I.
10.1023/A:1009043931968
Publisher site
See Article on Publisher Site

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.

Journal

Russian Journal of Plant PhysiologySpringer Journals

Published: Oct 10, 2004

References

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