Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.

@article{Brown1992RedesignedPY,
  title={Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.},
  author={Eric D Brown and Janet M Wood},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 18},
  pages={13086-92}
}
Proline utilization by Escherichia coli and Salmonella typhimurium requires expression of genes putP (encoding a proline transporter) and putA. Genetic data indicate that the PutA protein is both put repressor and a respiratory chain-linked dehydrogenase. We report a redesigned purification procedure as well as the physical characteristics and biological activities of the PutA protein purified from E. coli. The purified protein was homogeneous as determined by electrophoresis performed under… CONTINUE READING

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