Performance comparison of low-pressure ion-exchange chromatography media for protein separation

Levison, Peter R.; Mumford, Carol; Streater, Michael; Brandt-Nielsen, Anne; Pathirana, Navin D.; Badger, Stephen E.

doi:10.1016/s0021-9673(96)00814-x

Cited by 55 publications

(19 citation statements)

References 13 publications

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“…Using the data of the wet density of the Resin C (1.08 g. mL 1) and assuming a packed-bed voidage of 0.35 [17], it is estimated that the capacity of Resin C is 30.1 mg. mL 1 bed column. This value is higher than some commercially available biporous anion-exchange media for the same model protein [18].…”

Section: Adsorption Capacitymentioning

confidence: 63%

Development of rigid biporous polymeric adsorbent for protein chromatography

2002

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SummaryA novel biporous poly (glycidyl methacrylate-triallyl isocyanurate-divinylbenzene) resin (denoted as Resin C) was prepared by in-situ co-polymerization with both superfine granules of sodium sulfate and the solvents toluene and n-heptane as porogenic agents. This material is based on a novel porogenic mode of a combination of both solid granules and solvents. The properties of Resin C were characterized, and then compared with both Resin A (where only solvents as porogen) and Resin B (where only solid granules are used as porogen). The biporous resin showed good mechanical performance, high dynamic adsorption capacity and column efficiency at high flow-rates. These factors indicate the biporous resin as a promising adsorbent for high-speed protein separation by chromatography.

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Section: Adsorption Capacitymentioning

confidence: 63%

Development of rigid biporous polymeric adsorbent for protein chromatography

2002

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“…Using the data for the hydrated density of Resin B (Table I) and assuming a packed-bed voidage of 0.40 [17], it was estimated that the capacity of Resin B is 47.1 mg mL 1 bed column. This capacity value compares favorably with those of commercially available biporous anion-exchangers for the same model protein [18].…”

Section: Static Adsorption Equifibriummentioning

confidence: 73%

Fabrication and characterization of a novel biporous spherical adsorbent for protein chromatography

Shi

Sun

2003

Chromatographia

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SummaryA novel rigid spherical biporous poly(glyciclyl methacrylate-triallyl isocyanurate-clivinyJbenzene) resin (denoted Resin B) has been fabricated by radical suspension copolymerization, with superfine granules of calcium carbonate, and toluene and n-heptane, as porogenic agents, as the basis of a novel porogenic mode, cooperation of solid granules and solvents. The pore structure, static adsorption behavior, and chromatographic properties of Resin B were characterized and compared with those of Resin A (with only solvents as porogens). The results indicated that the biporous resin is a promising chromatographic medium for highspeed protein separation with good mechanical performance and high dynamic adsorption capacity ancl column efficiency at high flow rates.

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“…Due to the complexity of both the porous stationary phase structure and the protein structure and charge distribution, a priori prediction of the adsorption thermodynamics and transport rates in these systems remains elusive. Therefore, empirical methods are currently at the heart of the process development effort (Levison et al, 1997), increasing the costs associated with this stage of development. A complicating factor is that intraparticle transport rates are typically limiting, so transport rate data, in addition to static capacity measurements, are required to design the purification process successfully.…”

Section: Introductionmentioning

confidence: 99%

Effects of ionic strength on lysozyme uptake rates in cation exchangers. I: Uptake in SP Sepharose FF

Dziennik

Belcher

Barker

et al. 2005

Biotech & Bioengineering

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Fluorescence scanning confocal microscopy was used in parallel with batch uptake and breakthrough measurements of transport rates to study the effect of ionic strength on the uptake of lysozyme into SP Sepharose FF. In all cases the adsorption isotherms were near-rectangular. As described previously, the intraparticle profiles changed from slow-moving self-sharpening fronts at low salt concentration, to fast-moving diffuse profiles at high salt concentration, and batch uptake rates correspondingly increased with increasing salt concentration. Shrinking core and homogeneous diffusion frameworks were used successfully to obtain effective diffusivities for the low salt and high salt conditions, respectively. The prediction of column breakthrough was generally good using these frameworks, except for low-salt uptake results. In those cases, the compressibility of the stationary phase coupled with the shrinking core behavior appears to reduce the mass transfer rates at particle-particle contacts, leading to shallower breakthrough curves. In contrast, the fast uptake rates at high ionic strength appear to reduce the importance of mass transfer limitations at the particle contacts, but the confocal results do show a flow rate dependence on the uptake profiles, suggesting that external mass transfer becomes more limiting at high ionic strength. These results show that the complexity of behavior observable at the microscopic scale is directly manifested at the column scale and provides a phenomenological basis to interpret and predict column breakthrough. In addition, the results provide heuristics for the optimization of chromatographic conditions.

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Performance comparison of low-pressure ion-exchange chromatography media for protein separation

Cited by 55 publications

References 13 publications

Development of rigid biporous polymeric adsorbent for protein chromatography

Development of rigid biporous polymeric adsorbent for protein chromatography

Fabrication and characterization of a novel biporous spherical adsorbent for protein chromatography

Effects of ionic strength on lysozyme uptake rates in cation exchangers. I: Uptake in SP Sepharose FF

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