Hydrodynamic properties of porcine bestrophin-1 in Triton X-100.

@article{Stanton2006HydrodynamicPO,
  title={Hydrodynamic properties of porcine bestrophin-1 in Triton X-100.},
  author={James Brett Stanton and Andrew F X Goldberg and George Hoppe and Lihua Y. Marmorstein and Alan D. Marmorstein},
  journal={Biochimica et biophysica acta},
  year={2006},
  volume={1758 2},
  pages={241-7}
}
Bestrophin-1 (Best-1) is an integral membrane protein, defects in which cause Best vitelliform macular dystrophy. Best-1 is proposed to function as a Cl- channel and/or a regulator of Ca++ channels. A tetrameric (or pentameric) stoichiometry has been reported for recombinant best-1. Using a combination of gel exclusion chromatography and velocity sedimentation we examined the quaternary structure of native best-1 and found that it migrates as a single species with a Stokes radius of 7.3 nm… CONTINUE READING

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