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

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.