Kinetics of the reconstituted dicarboxylate carrier from rat liver mitochondria
作者： C. Indiveri , L. Capobianco , R. Krämer , F. Palmieri
DOI: 10.1016/S0005-2728(89)80070-2
关键词:
摘要: The dicarboxylate carrier from rat liver mitochondria was purified by the Amberlite/hydroxyapatite procedure and reconstituted in egg yolk phospholipid vesicles removing detergent with Amberlite. efficiency of reconstitution optimized respect to ratio detergent/phospholipid, concentration number Amberlite column passages. In system incorporated catalyzed a first-order reaction malate/phosphate exchange. V exchange determined be 6000 μmol/min per g protein at 25°C. This value independent type substrate present external or internal space liposomes (malate, phosphate malonate). half-saturation constant 0.49 mM for malate, 0.54 malonate 1.41 phosphate. activation energy 95.8 kJ/mol. transport pH range between 6 8.
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