ATP synthesis by purified ATP-synthase from beef heart mitochondria after coreconstitution with bacteriorhodopsin.

@article{Matuschka1995ATPSB,
  title={ATP synthesis by purified ATP-synthase from beef heart mitochondria after coreconstitution with bacteriorhodopsin.},
  author={S Matuschka and Klaus Zwicker and Thomas Nawroth and G. Zimmer},
  journal={Archives of biochemistry and biophysics},
  year={1995},
  volume={322 1},
  pages={135-42}
}
An ATP-synthase complex active in ATP synthesis was isolated from beef heart mitochondria by solubilization of submitochondrial particles with dodecyl-beta-D-maltoside and purified in a one-step procedure by subsequent ion-exchange chromatography. The electrophoretic analysis resulted in 14 subunits for the F0 F1 complex. ATP hydrolysis activity of the purified enzyme was 25 mumol ATP min-1 mg-1F0F1. ATP hydrolysis could be stimulated by addition of lipid vesicles. Further stimulation was… CONTINUE READING