Purification and characterization of the aspartate chemoreceptor.

@article{Foster1985PurificationAC,
  title={Purification and characterization of the aspartate chemoreceptor.},
  author={Douglas L. Foster and Sherry L Mowbray and Bing K. Jap and Daniel E. Koshland},
  journal={The Journal of biological chemistry},
  year={1985},
  volume={260 21},
  pages={11706-10}
}
The chemoreceptor for aspartate in Salmonella typhimurium was purified from an Escherichia coli strain containing a plasmid bearing the receptor's structural gene (tar). The receptor was solubilized from salt-washed membranes with the nonionic detergent octyl-beta-D-glucopyranoside and purified by a combination of ion exchange, molecular sieve and hydroxyapatite-agarose chromatography. The inclusion of glycerol and 1,10-phenanthroline in all buffers used prior to ion exchange chromatography… CONTINUE READING