Dye removal, catalytic activity and 2D crystallization of chloroplast H(+)-ATP synthase purified by blue native electrophoresis.

@article{Poetsch2000DyeRC,
  title={Dye removal, catalytic activity and 2D crystallization of chloroplast H(+)-ATP synthase purified by blue native electrophoresis.},
  author={Ansgar Poetsch and Dirk Neff and Holger Seelert and Hermann Sch{\"a}gger and Norbert A. Dencher},
  journal={Biochimica et biophysica acta},
  year={2000},
  volume={1466 1-2},
  pages={339-49}
}
The proton-ATP synthase of thylakoid membranes from spinach chloroplasts (CF(O)F(1)) and its subcomplexes CF(O) and CF(1) were isolated by blue native electrophoresis (BN-PAGE) [Neff, D. and Dencher, N.A. (1999) Biochem. Biophys. Res. Commun. 259, 569-575] and subsequently electroeluted from the gel. A method was developed to remove most of the dye Coomassie G-250 (CBG) using gel filtration, a prerequisite for many biophysical investigations. The dye was removed from the electroeluted CF(O)F(1… CONTINUE READING
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