The multidrug resistance half-transporter ABCG2 is purified as a tetramer upon selective extraction from membranes.

@article{Dezi2010TheMR,
  title={The multidrug resistance half-transporter ABCG2 is purified as a tetramer upon selective extraction from membranes.},
  author={Manuela Dezi and Pierre-Fr{\'e}deric Fribourg and Aur{\'e}lie Di Cicco and Oph{\'e}lie Arnaud and Sergio Di Marco and Pierre Guy Falson and Attilio di Pietro and Daniel L{\'e}vy},
  journal={Biochimica et biophysica acta},
  year={2010},
  volume={1798 11},
  pages={2094-101}
}
ABCG2 is a human membrane ATP-binding cassette half-transporter that hydrolyzes ATP to efflux a large number of chemotherapeutic agents. Several oligomeric states of ABCG2 from homodimers to dodecamers have been reported depending on the overexpression systems and/or the protocols used for purification. Here, we compared the oligomeric state of His(6)-ABCG2 expressed in Sf9 insect cells and in human Flp-In-293/ABCG2 cells after solubilization in mild detergents. His(6)-ABCG2 was purified… CONTINUE READING