Interaction of the Escherichia coli trp aporepressor with its ligand, L-tryptophan.

@article{Arvidson1986InteractionOT,
  title={Interaction of the Escherichia coli trp aporepressor with its ligand, L-tryptophan.},
  author={Dennis N. Arvidson and Can Bruce and Robert P. Gunsalus},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 1},
  pages={238-43}
}
We have examined the interaction of the Escherichia coli trp aporepressor with its ligand, L-tryptophan, using both equilibrium dialysis and flow dialysis methods. Results obtained by the two procedures were equivalent and indicate that the trp aporepressor binds L-tryptophan with an equilibrium dissociation constant (Kd) of 40 microM at 25 degrees C under standard binding assay conditions (10 mM potassium phosphate, pH 7.4, 0.2 M potassium chloride, 0.1 mM EDTA, 5% glycerol). Molecular sizing… CONTINUE READING