Purification and characterization of the F1-ATPase from Clostridium thermoaceticum.

@article{Ivey1986PurificationAC,
  title={Purification and characterization of the F1-ATPase from Clostridium thermoaceticum.},
  author={Douglas Ivey and Lars G. Ljungdahl},
  journal={Journal of bacteriology},
  year={1986},
  volume={165 1},
  pages={
          252-7
        }
}
The F1 portion of the H+-ATPase from Clostridium thermoaceticum was purified to homogeneity by solubilization at low ionic strength, ion-exchange chromatography, and gel filtration. The last indicated the Mr to be 370,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the pure enzyme revealed four bands with Mr corresponding to 60,000, 55,000, 37,000, and 17,000 in an apparent molar ratio of 3:3:1:1. The purified enzyme would bind to stripped membranes to reconstitute… CONTINUE READING
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