Properties of mitochondria and peroxisomal enoyl-CoA hydratases from rat liver.

@article{Furuta1980PropertiesOM,
  title={Properties of mitochondria and peroxisomal enoyl-CoA hydratases from rat liver.},
  author={S. Furuta and S. Miyazawa and T. Osumi and T. Hashimoto and N. Ui},
  journal={Journal of biochemistry},
  year={1980},
  volume={88 4},
  pages={
          1059-70
        }
}
  • S. Furuta, S. Miyazawa, +2 authors N. Ui
  • Published 1980
  • Biology, Medicine
  • Journal of biochemistry
  • Mitochondrial and peroxisomal enoyl-CoA hydratases were purified from rat liver. The mitochondrial enzyme, with a molecular weight of 161,000, was composed of 6 identical subunits. The molecular structure of the rat liver enzyme was very similar to that of the bovine liver enzyme. Acetoacetyl-CoA was a competitive inhibitor of the mitochondrial enzymes. The results of titration of the rat liver enzyme with acetoacetyl-CoA suggest that 3 subunits of the enzyme exhibit catalytic activity. The… CONTINUE READING
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