Electrophoretic mobilities of proteins and protein mixtures

https://doi.org/10.1016/0009-2509(94)00434-SGet rights and content

Abstract

Electrophoretic mobilities of bovine serum albumin (SA), haemoglobin (Hb) and ovalbumin (OA) have been determined by direct ultramicroscopic observation of the velocities of individual particles in a particle electrophoresis apparatus, and of SA and Hb in a free-flow apparatus of the type described independently by Hannig and by Strickler. Agreement between the results obtained by the two methods for SA and Hb over wide pH ranges covering both sides of the respective isoelectric points was surprisingly good. Runs were also conducted in the free-flow cell in which SA was transported in buffer containing Hb, and vice versa; these showed clear evidence of interactions between the motions of the two proteins, as occurs in the parallel case of multicomponent diffusion, but the results could not be quantified in terms of the Maxwell-Stefan theory. Finally, the single protein data were compared with predictions made on the basis of the Debye-Huckel-Henry theory, and showed reasonable agreement.

References (46)

  • V.P. Dole

    The electrophoretic patterns of normal plasma

    J. Clin. Invest.

    (1944)
  • N.G. Douglas

    Electrophoretic mobilities of proteins and protein mixtures in solution

  • N.G. Douglas et al.

    Electrophoretic mobilities of proteins in free solution

  • P. Dunnill

    Trends in downstream processing of proteins and enzymes

    Process Biochem.

    (1983)
  • N.B. Egen et al.
  • K. Hannig

    Preparative electrophoresis

  • K. Hannig
  • K. Hannig
  • K. Hannig
  • K. Hannig
  • K. Hannig et al.

    Free-flow electrophoresis III. An analytical version for a rapid, quantitative determination of electrophoretic parameters

    Hoppe-Seyler Z. Physiol. Chem.

    (1977)
  • G.S. Hartley

    Theory of the velocity of diffusion of strong electrolytes in dilute solutions

    Phil. Mag.

    (1931)
  • D.C. Henry

    The cataphoresis of suspended particles—I. The equation of cataphoresis

  • Cited by (28)

    • Laser Doppler Electrophoresis applied to colloids and surfaces

      2015, Current Opinion in Colloid and Interface Science
      Citation Excerpt :

      Furthermore the higher electrolyte concentration rendered anodic protein degradation to negligible levels and, following an extended course of zeta potential measurements, DLS on the recovered protein sample confirmed no change in hydrodynamic diameter due to the process. In addition, the compact format of the folded capillary cell has enabled useful measurements concerning protein conformation over the temperature range 15 to 75 °C, and on BSA the recorded mobility values (below the aggregation point) were found to be in good agreement with those obtained using both capillary and free-flow electrophoresis [19,20]. This is an important advance in the measurement of Protein Electrokinetic properties.

    • Effective charge of bovine serum albumin determined by electrophoresis NMR

      2007, Chemical Physics Letters
      Citation Excerpt :

      There maybe as well binding of the buffer ions to the protein [19,20]. Evaluated charges resulting from other electrophoretic measurements like electrophoretic light scattering [21], free-flow electrophoresis [22] or capillary electrophoresis [23] however are in good agreement with data of E-NMR. Small discrepancies arise from differences in concentration and ionic strength of the protein solution used in detail for investigation.

    View all citing articles on Scopus
    View full text