Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae.

@article{Andi2004StabilizationAC,
  title={Stabilization and characterization of histidine-tagged homocitrate synthase from Saccharomyces cerevisiae.},
  author={Babak Andi and Ann H. West and Paul F. Cook},
  journal={Archives of biochemistry and biophysics},
  year={2004},
  volume={421 2},
  pages={243-54}
}
Histidine-tagged homocitrate synthase from Saccharomyces cerevisiae was purified to about 98% using a Ni-NTA resin and stabilized using a combination of 100 mM guanidine hydrochloride, 100 mM alpha-cyclodextrin, and 600 mM ammonium sulfate. The enzyme was assayed using dichlorophenol indophenol (DCPIP) as an oxidant to oxidize the CoASH produced in the reaction. A stoichiometry of 1:1 was obtained between DCPIP and CoASH. Kinetic parameters for the stable enzyme at pH 7.5 are: Km (AcCoA), 24… CONTINUE READING
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