Purification and characterization of acetoacetyl-CoA synthetase from rat liver.

@article{Ito1984PurificationAC,
  title={Purification and characterization of acetoacetyl-CoA synthetase from rat liver.},
  author={Masaaki Ito and Toshio Fukui and Makoto c Kamokari and Takuya Saito and Keiichi Tomita},
  journal={Biochimica et biophysica acta},
  year={1984},
  volume={794 2},
  pages={
          183-93
        }
}
Acetoacetyl-CoA synthetase (acetoacetate:CoA ligase) was purified to electrophoretic homogeneity from a rat liver supernatant by ammonium sulfate fractionation and successive chromatographies on DEAE-Sepharose, Blue-Sepharose, Red-Sepharose, CoA-Sepharose, Ultrogel AcA-44, and DEAE-Sepharose once again. The purified enzyme had a specific activity of 2.3 mumol acetoacetyl-CoA formed per min per mg protein, which constituted a 960-fold purification compared to the crude extract, with a 7.4% yield… CONTINUE READING

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