Molecular and catalytic properties of mitochondrial (ketogenic) 3-hydroxy-3-methylglutaryl coenzyme A synthase of liver.

@article{Reed1975MolecularAC,
  title={Molecular and catalytic properties of mitochondrial (ketogenic) 3-hydroxy-3-methylglutaryl coenzyme A synthase of liver.},
  author={William D. Reed and D Clinkenbeard and Melissa D. Lane},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 8},
  pages={3117-23}
}
Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase has been purified to homogeneity from avian liver. The enzyme in dilute phosphate buffer, pH 7.0, has an S20,w of 5.7 S and a molecular weight of 105,000 determined by sedimentation equilibrium; the presence of 0.1 M KCl causes dissociation to a form one-half that size, i.e. about 57,000 daltons. Since the subunit molecular weight of the synthase determined by the dodecyl sulfate acrylamide gel method is 53,000, it appears that the native… CONTINUE READING