Electrostatic effects on protein partitioning in size-exclusion chromatography and membrane ultrafiltration

Journal of Chromatography. a
N S Pujar, A L Zydney

Abstract

Although size-exclusion chromatography and membrane ultrafiltration are generally viewed as size-based separation processes, there is considerable evidence for the importance of electrostatic interactions. Experimental studies of size-exclusion chromatography and membrane ultrafiltration were performed in parallel using both neutral dextrans and charged proteins. Data for protein retention time and membrane sieving clearly indicate that the effective protein size increases with decreasing ionic strength due to the reduction in electrostatic shielding. These results were quantified using available theoretical models for the partitioning of charged solutes. The data clearly demonstrate the similarity of the electrostatic interactions and partitioning effects in size-exclusion chromatography and membrane ultrafiltration.

References

Nov 20, 1995·Biotechnology and Bioengineering·R H van EijndhovenA L Zydney

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Citations

Feb 3, 2009·Annals of Biomedical Engineering·A T ConliskShuvo Roy
Feb 26, 2004·Journal of Biochemical and Biophysical Methods·Leopold K KostanskiArchie E Hamielec
Nov 7, 2009·Journal of Pharmaceutical Sciences·Tsutomu ArakawaJohn S Philo
May 7, 2010·Journal of Chromatography. a·Tiago VicenteManuel J T Carrondo
Dec 25, 2009·Journal of Chromatography. a·Stephanie JungUlrich Tallarek
Jul 11, 2009·Journal of Colloid and Interface Science·Panadda Dechadilok, William M Deen
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