Diffusion and partitioning of proteins in charged agarose gels.

@article{Johnson1995DiffusionAP,
  title={Diffusion and partitioning of proteins in charged agarose gels.},
  author={Erin M. Johnson and David A. Berk and Rakesh K. Jain and William M. Deen},
  journal={Biophysical journal},
  year={1995},
  volume={68 4},
  pages={
          1561-8
        }
}
The effects of electrostatic interactions on the diffusion and equilibrium partitioning of fluorescein-labeled proteins in charged gels were examined using fluorescence recovery after photobleaching and gel chromatography, respectively. Measurements were made with BSA, ovalbumin, and lactalbumin in SP-Sepharose (6% sulfated agarose), in phosphate buffers at pH 7 and ionic strengths ranging from 0.01 to 1.0 M. Diffusivities in individual gel beads (D) and in the adjacent bulk solution (D… CONTINUE READING

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