The ATP synthetase of Escherichia coli K12: purification of the enzyme and reconstitution of energy-transducing activities.

@article{Friedl1979TheAS,
  title={The ATP synthetase of Escherichia coli K12: purification of the enzyme and reconstitution of energy-transducing activities.},
  author={Peter Friedl and C Friedl and Hans Ulrich Schairer},
  journal={European journal of biochemistry},
  year={1979},
  volume={100 1},
  pages={175-80}
}
The ATP synthetase of Escherichia coli K12 was purified by a simple procedure. The dicyclohexylcarbodiimide-sensitive ATPase activity was enriched 21-fold. The ATP synthetase preparation contained the eight polypeptides (alpha, beta, gamma, a,delta, b,espilon, c) of the enzyme and a residual contamination (4% of the total protein) as shown by dodecylsulfate/polyacrylamide electrophoresis. The polypeptide c was specifically labelled with [14C]dicyclohexylcarbodiimide. Energy-transducing… CONTINUE READING