Electrophoretic mobilities of proteins and protein mixtures
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Laser Doppler Electrophoresis applied to colloids and surfaces
2015, Current Opinion in Colloid and Interface ScienceCitation 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.
Rigorous estimation of effective protein charge from experimental electrophoretic mobilities for proteomics analysis using microchip electrophoresis
2008, Colloids and Surfaces A: Physicochemical and Engineering AspectsEffective charge of bovine serum albumin determined by electrophoresis NMR
2007, Chemical Physics LettersCitation 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.
Protein separation on a technical scale using a radial symmetric free flow zone electrophoresis cell
2005, Chemical Engineering ScienceBinary oscillatory cross-flow electrophoresis: Theory and experiments
1998, Journal of Pharmaceutical Sciences