Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes.

@article{Rokosz1994HumanC3,
  title={Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes.},
  author={L L Rokosz and Dr A. J. M. Boulton and E A Butkiewicz and Gautam Sanyal and Mar{\'i}a Ang{\'e}lica Cueto and Paul LaChance and Jeffrey D. Hermes},
  journal={Archives of biochemistry and biophysics},
  year={1994},
  volume={312 1},
  pages={1-13}
}
A cDNA for the human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) synthase (EC 4.1.3.5) was subcloned and expressed from a T7-based vector in Escherichia coli. The over-produced enzyme was purified using a three-step protocol that generated 20 to 30 mg protein/liter cell culture. The physical and catalytic properties of the recombinant synthase are similar to those reported for the nonrecombinant enzymes from chicken liver [Clinkenbeard et al. (1975a) J. Biol. Chem. 250, 3124… CONTINUE READING
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