Effect of salts and temperature on the adsorption of bovine serum albumin on polypropylene glycol-Sepharose under linear and overloaded chromatographic conditions

Dias-Cabral, A.C.; Queiroz, João A.; Pinto, Neville G.

doi:10.1016/j.chroma.2003.07.010

Cited by 39 publications

(30 citation statements)

References 29 publications

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“…This figure summarizes the effects of both temperature and (NH 4 ) 2 SO 4 concentration. The values with PPGSepharose (n = 3) are also shown for comparison; these were reported in an earlier publication (Dias-Cabral et al, 2003). For both supports the data obtained were very reproducible.…”

Section: Linear Regionsupporting

confidence: 63%

“…As reported earlier (Dias-Cabral et al, 2003), experimental data indicate that changes in protein conformation influence the process. On the basis of PPG (n = 7) results obtained, it is likely that this ligand also changes its Adsorption of bovine serum albumin onto polypropyleneglycol-Sepharose 609 ORIGINAL RESEARCH conformation within the range of conditions studied (Yarovsky et al, 1995).…”

Section: Linear Regionmentioning

confidence: 65%

“…An important measurement, one that can reflect changes in contact area, and is a sensitive measure of protein conformation (Wu et al, 1986;Dias-Cabral et al, 2003), is the number of water molecules displaced per protein molecule adsorbed (Z). The Z value can be obtained from equation (1) (Geng et al, 1990).…”

Section: Linear Regionmentioning

confidence: 99%

“…K is the equilibrium constant, L d corresponds to the hydrated ligands in salt solution, n′ is the number of ligand interactions with a protein molecule and φ is the column phase ratio. For a given chromatographic system, when the salt, ligand and temperature are fixed, Z is a characteristic constant related to protein conformation (Dias-Cabral et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

“…It has been demonstrated previously that calorimetry provides valuable insight for overloaded protein chromatography. The equilibrium adsorption is dictated by the Gibbs free energy change for adsorption (∆G ads ), which is dependent upon the overall enthalpy change (∆ H ads ), which can be calculated from the heat of adsorption (Esquibel-King et al, 1999;Thrash and Pinto, 2001;Dias-Cabral et al, 2002, 2003Thrash and Pinto, 2002).…”

Section: Introductionmentioning

confidence: 99%

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The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol–Sepharose

Dias-Cabral

Ferreira

Phillips

et al. 2005

Biomedical Chromatography

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The interaction thermodynamics associated with bovine serum albumin adsorption on polypropylene glycol (n=3)-Sepharose CL-6B and polypropylene glycol (n=7)-Sepharose CL-6B, using ammonium sulfate as the modulator was studied. Analysis of data under linear conditions was accomplished with the stoichiometric displacement retention model, preferential interaction approach and van't Hoff plots applied to HIC systems. Preferential interaction analysis indicated a strong entropic driving force under linear conditions, due to the release of a large amount of solvent on adsorption. In contrast, flow microcalorimetry under overloaded conditions showed that the adsorption of bovine serum albumin may be entropically or enthalpically driven. It is postulated that adsorption in the nonlinear region is influenced by the degree of water release, protein-protein interactions on the surface, reorientation of ligand, and conformational changes in the protein.

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Section: Linear Regionsupporting

confidence: 63%

Section: Linear Regionmentioning

confidence: 65%

Section: Linear Regionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol–Sepharose

Dias-Cabral

Ferreira

Phillips

et al. 2005

Biomedical Chromatography

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Temperature‐induced conformational transition of bovine serum albumin in neutral aqueous solution by reversed‐phase liquid chromatography

Bian

2013

Biomedical Chromatography

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The temperature-induced conformational transition of bovine serum albumin (BSA) in neutral aqueous solution was studied using intrinsic fluorescence emission spectrum, reversed-phase liquid chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and the conformation transition thermodynamic parameters were determined in the temperature range 12-50°C. The results showed that, in the temperature range 12-20°C, BSA only existed in a single conformation state A, while in the temperature range 22-50°C, it existed in two different conformation states: A and B. The percentage of conformation state A decreased while that of conformation state B increased with the increase in temperatures, and when temperature approached 50°C conformation state B accounted for approximately 25% of all conformation states of BSA. In the conformational transition of BSA from conformation state A to conformation state B, the positive enthalpy change, entropy change and free energy changes demonstrated that the conformational transition was endothermic, nonspontaneous and mainly entropy-driven.

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Roles of interstitial fraction and load conditions on the dynamic binding capacity of proteins on capillary‐channeled polymer fiber columns

Wang

Marcus

2014

Biotechnology Progress

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Capillary-channeled polymer (C-CP) fibers are used as a stationary phase for ion-exchange chromatography of proteins. Collinear packing of the fibers permits operation at high linear velocities (Uo > 100 mm s(-1)) and low backpressure (<2,000 psi) on analytical-scale columns. Rapid solvent transport is matched with very efficient solute mass transfer as fibers are virtually non-porous with respect to the size of the target protein molecules. Lack of porosity of course limits the equilibrium binding capacity of stationary phases. Breakthrough curves and frontal analysis are used to better understand trade-offs between the kinetic and thermodynamic properties as C-CP fibers are applied in preparative situations. Fiber columns packed to different interstitial fraction values affect both the total fiber surface area (e.g., equilibrium binding capacity [EBC]) and the permittivity to flow and mass transport characteristics (e.g., dynamic binding capacity [DBC]). The EBC of the nylon 6 C-CP fibers was found to be 1.30 mg g(-1), with isotherms that were best matched by a Moreau model, showing linearity up to solute concentrations of ∼0.4 mg mL(-1). Isotherms generated under flow conditions were equally well approximated using Langmuir, Freundlich, and Moreau isotherm models. Fairly linear responses were seen up to the maximum load concentration of 1.2 mg mL(-1). Counterintuitively, dynamic studies revealed that conditions of high column porosity yielded a DBC that is ∼70% higher than the EBC. These findings point to potential advantages in terms downstream processing applications, where protein throughput and yield are critical metrics.

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Effect of salts and temperature on the adsorption of bovine serum albumin on polypropylene glycol-Sepharose under linear and overloaded chromatographic conditions

Cited by 39 publications

References 29 publications

The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol–Sepharose

The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol–Sepharose

Temperature‐induced conformational transition of bovine serum albumin in neutral aqueous solution by reversed‐phase liquid chromatography

Roles of interstitial fraction and load conditions on the dynamic binding capacity of proteins on capillary‐channeled polymer fiber columns

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