Catalytic properties of Escherichia coli F1-ATPase depleted of endogenous nucleotides.

@article{Senior1992CatalyticPO,
  title={Catalytic properties of Escherichia coli F1-ATPase depleted of endogenous nucleotides.},
  author={Alan E. Senior and Rhee Suhk Lee and Marwan K Al-Shawi and Joachim Weber},
  journal={Archives of biochemistry and biophysics},
  year={1992},
  volume={297 2},
  pages={340-4}
}
Nucleotide-depleted Escherichia coli F1 was prepared by the procedure of Wise et al. (1983, Biochem. J. 215, 343-350). This enzyme had high rates of steady-state ATPase and GTPase activity. When "unisite" ATP hydrolysis was measured using an F1/ATP concentration ratio of 10, all of the substoichiometric ATP became bound to the high-affinity catalytic site… CONTINUE READING