Expression, purification, and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli. Kinetic evidence that the E. coli mannitol transport protein is a functional dimer.

@article{Boer1994ExpressionPA,
  title={Expression, purification, and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli. Kinetic evidence that the E. coli mannitol transport protein is a functional dimer.},
  author={Harry Boer and R H ten Hoeve-Duurkens and Gea K. Schuurman-Wolters and Arnoud Jan Dijkstra and George T. Robillard},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 27},
  pages={17863-71}
}
The overexpression of the membrane-bound C domain of the mannitol transport protein EIIMtl of Escherichia coli has been achieved. This protein, IICMtl, consisting of the first 346 amino acids, was purified from membrane vesicles and still bound mannitol with a high affinity. Gel filtration experiments showed that purified IICMtl was a dimer, confirming that the interaction within the EIIMtl dimer occurs between the membrane-bound portions of the protein. IICMtl in combination with a chimeric… CONTINUE READING

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