A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase.

@article{Xu2004ASO,
  title={A study of the relationships of interactions between Asp-201, Na+ or K+, and galactosyl C6 hydroxyl and their effects on binding and reactivity of beta-galactosidase.},
  author={Julia Xu and Mary A A McRae and Scott A. Harron and Beatrice Rob and Reuben E Huber},
  journal={Biochemistry and cell biology = Biochimie et biologie cellulaire},
  year={2004},
  volume={82 2},
  pages={275-84}
}
The interactions between Na+ (and K+) and Asp-201 of beta-galactosidase were studied. Analysis of the changes in Km and Vmax showed that the Kd for Na+ of wild type beta-galactosidase (0.36 +/- 0.09 mM) was about 10x lower than for K+ (3.9 +/- 0.6 mM). The difference is probably because of the size and other physical properties of the ions and the binding… CONTINUE READING