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

  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},
  volume={1758 2},
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


Publications citing this paper.
Showing 1-10 of 20 extracted citations


Publications referenced by this paper.
Showing 1-10 of 42 references


  • A. D. Marmorstein, L. Y. Marmorstein, M. Rayborn, X. Wang, J. G. Hollyfield, K. Petrukhin
  • the product of the Best vitelliform macular…
  • 2000
Highly Influential
12 Excerpts

Chader (Eds.), Progress in Retinal Research

  • R. H. Steinberg, R. A. Linsenmeier, E. R. Griff, G. J. in N.N. Osborne
  • 1985
Highly Influential
4 Excerpts


  • M. Chabre
  • le Maire, Monomeric G-protein-coupled receptor as…
  • 2005
1 Excerpt

Similar Papers

Loading similar papers…