Functional comparison of mouse slc26a6 anion exchanger with human SLC26A6 polypeptide variants: differences in anion selectivity, regulation, and electrogenicity.

@article{Chernova2005FunctionalCO,
  title={Functional comparison of mouse slc26a6 anion exchanger with human SLC26A6 polypeptide variants: differences in anion selectivity, regulation, and electrogenicity.},
  author={Marina N. Chernova and Lianwei Jiang and David J. Friedman and Rachel B Darman and Hannes T Lohi and Juha Kere and David H. Vandorpe and Seth L Alper},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 9},
  pages={8564-80}
}
The unusually low 78% amino acid identity between the orthologous human SLC26A6 and mouse slc26a6 polypeptides prompted systematic comparison of their anion transport functions in Xenopus oocytes. Multiple human SLC26A6 variant polypeptides were also functionally compared. Transport was studied as unidirectional fluxes of (36)Cl(-), [(14)C]oxalate, and [(35)S]sulfate; as net fluxes of HCO(3)(-) by fluorescence ratio measurement of intracellular pH; as current by two-electrode voltage clamp; and… CONTINUE READING
56 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 56 extracted citations

Similar Papers

Loading similar papers…