Purification and functional reconstitution of the 2-oxoglutarate/malate translocator from spinach chloroplasts.

@article{Menzlaff1993PurificationAF,
  title={Purification and functional reconstitution of the 2-oxoglutarate/malate translocator from spinach chloroplasts.},
  author={E Menzlaff and Ulf Ingo Fl{\"u}gge},
  journal={Biochimica et biophysica acta},
  year={1993},
  volume={1147 1},
  pages={13-8}
}
The chloroplast 2-oxoglutarate/malate translocator was solubilized from envelope membranes by the detergent n-dodecyl beta-D-maltoside and purified to apparent homogeneity by anion-exchange chromatography followed by gel permeation chromatography. During the purification procedure, the activity of the translocator was monitored by functional reconstitution into phospholipid vesicles. The purified translocator protein has an apparent molecular mass of about 45,000 as revealed by SDS-PAGE. Based… CONTINUE READING