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

Pujar, Narahari S.; Zydney, Andrew L.

doi:10.1016/s0021-9673(97)01003-0

Cited by 102 publications

(74 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Such a hypothesis may provide a path to reconciling present findings with a wider range of media and proteins as well as the work of earlier scientists (e.g., Dziennik et al, 2003;Pujar and Zydney, 1998) and the obvious complexity of protein transport and binding in charged hydrogels (Carlsson et al, 2001;Lewus and Carta, 2001;Liapis et al, 2001).…”

Section: Discussionmentioning

confidence: 53%

See 1 more Smart Citation

An exclusion mechanism in ion exchange chromatography

Harinarayan

Mueller

Ljunglöf³

et al. 2006

Biotech & Bioengineering

136

107

View full text Add to dashboard Cite

Protein dynamic binding capacities on ion exchange resins are typically expected to decrease with increasing conductivity and decreasing protein charge. There are, however, conditions where capacity increases with increasing conductivity and decreasing protein charge. Capacity measurements on two different commercial ion exchange resins with three different monoclonal antibodies at various pH and conductivities exhibited two domains. In the first domain, the capacity unexpectedly increased with increasing conductivity and decreasing protein charge. The second domain exhibited traditional behavior. A mechanism to explain the first domain is postulated; proteins initially bind to the outer pore regions and electrostatically hinder subsequent protein transport. Such a mechanism is supported by protein capacity and confocal microscopy studies whose results suggest how knowledge of the two types of IEX behavior can be leveraged in optimizing resins and processes. ß

show abstract

Section: Discussionmentioning

confidence: 53%

“…Exclusion effects seen in SEC and membranes have been correlated (Pujar and Zydney, 1998). Pujar and Zydney (1998) demonstrated the similarity of the electrostatic exclusion occurring in both by determining retention times in SEC and sieving coefficients in ultrafiltration membranes for BSA and dextrans.…”

Section: Introductionmentioning

confidence: 95%

An exclusion mechanism in ion exchange chromatography

Harinarayan

Mueller

Ljunglöf³

et al. 2006

Biotech & Bioengineering

136

107

View full text Add to dashboard Cite

show abstract

“…When the pH of the ovalbumin solution was varied, the evaluated diameter of ovalbumin molecules became the smallest at the isoelectric point of ovalbumin (i.e., pH 4.6). This variation of the diameter with pH was attempted to explain based on a model modified from that proposed by Pujar and Zydney [33]. It was found that the experimentally obtained value of the diameter can almost be reproduced by the calculation on the basis of the modified model.…”

Section: Discussionmentioning

confidence: 92%

“…(6), (7) and (8) by Pujar and Zydney [33] can also be applied to the estimation of the effective diameter of ovalbumin molecules adsorbed on bubble surfaces in the saturated state. A further study will be necessary about the relation between the saturated adsorption state of foams and their stabilities.…”

Section: Variation Of Effective Diameter For Ovalbumin On the Bubble mentioning

confidence: 99%

Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation

Maruyama

Seki

Suzuki

et al. 2006

Journal of Colloid and Interface Science

View full text Add to dashboard Cite

show abstract

“…At a pH above the pI, the protein is negatively charged; at a pH below the pI, the protein is positively charged. Proteins are large biomolecules and can thus be heavily charged (BSA's net charge is À 13 at pH 7) 42 . Strong electrostatic interactions between proteins and charged particles were therefore expected.…”

Section: Preparation and Characterization Of Nanoporous Particlesmentioning

confidence: 99%

Biomimetic block copolymer particles with gated nanopores and ultrahigh protein sorption capacity

et al. 2014

View full text Add to dashboard Cite

The design of micro-or nanoparticles that can encapsulate sensitive molecules such as drugs, hormones, proteins or peptides is of increasing importance for applications in biotechnology and medicine. Examples are micelles, liposomes and vesicles. The tiny and, in most cases, hollow spheres are used as vehicles for transport and controlled administration of pharmaceutical drugs or nutrients. Here we report a simple strategy to fabricate microspheres by block copolymer self-assembly. The microsphere particles have monodispersed nanopores that can act as pH-responsive gates. They contain a highly porous internal structure, which is analogous to the Schwarz P structure. The internal porosity of the particles contributes to their high sorption capacity and sustained release behaviour. We successfully separated similarly sized proteins using these particles. The ease of particle fabrication by macrophase separation and self-assembly, and the robustness of the particles makes them ideal for sorption, separation, transport and sustained delivery of pharmaceutical substances.

show abstract

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

Cited by 102 publications

References 21 publications

An exclusion mechanism in ion exchange chromatography

An exclusion mechanism in ion exchange chromatography

Variation of saturated surface density of ovalbumin on bubble surface in continuous foam separation

Biomimetic block copolymer particles with gated nanopores and ultrahigh protein sorption capacity

Contact Info

Product

Resources

About