CTP synthetase from Escherichia coli: an improved purification procedure and characterization of hysteretic and enzyme concentration effects on kinetic properties.

@article{Anderson1983CTPSF,
  title={CTP synthetase from Escherichia coli: an improved purification procedure and characterization of hysteretic and enzyme concentration effects on kinetic properties.},
  author={Paul M. Anderson},
  journal={Biochemistry},
  year={1983},
  volume={22 13},
  pages={3285-92}
}
Previous studies have shown that CTP synthetase exists as a dimer which aggregates to a tetramer in the presence of the substrates ATP and UTP [Long, C. W., Levitzki, A., & Koshland, D. E., Jr. (1970) J. Biol. Chem. 245, 80]. A new, relatively simple purification procedure resulting in enzyme of high purity and in good yield has been established by using two successive hydrophobic chromatography steps, the first in the absence of ATP and UTP (dimer binds) and the second in the presence of ATP… CONTINUE READING

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