2007
DOI: 10.1002/bp070092x
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Analysis of the Statistical Thermodynamic Model for Nonlinear Binary Protein Adsorption Equilibria

Abstract: The statistical thermodynamic (ST) model was used to study nonlinear binary protein adsorption equilibria on an anion exchanger. Single-component and binary protein adsorption isotherms of bovine hemoglobin (Hb) and bovine serum albumin (BSA) on DEAE Spherodex M were determined by batch adsorption experiments in 10 mM Tris-HCl buffer containing a specific NaCl concentration (0.05, 0.10, and 0.15 M) at pH 7.40. The ST model was found to depict the effect of ionic strength on the single-component equilibria well… Show more

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Cited by 5 publications
(5 citation statements)
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“…With an increase of salt concentration, both k 11 and k 22 decreased gradually due to the screening effect by co‐ions was strengthened and the electrostatic repulsion of adsorbed protein molecules became weaker. The same tendency was reported previously by Zhou et al . However, k 22 did not follow this pattern as salt concentration increased from 50 to 100 mmol/L.…”
Section: Resultssupporting
confidence: 89%
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“…With an increase of salt concentration, both k 11 and k 22 decreased gradually due to the screening effect by co‐ions was strengthened and the electrostatic repulsion of adsorbed protein molecules became weaker. The same tendency was reported previously by Zhou et al . However, k 22 did not follow this pattern as salt concentration increased from 50 to 100 mmol/L.…”
Section: Resultssupporting
confidence: 89%
“…Among three isothermal models, values of q BSA were underestimated by SMA model while calculated values of q BSA by ST model were higher than those by other two models. These tendencies in SMA and ST models were also found by previous researches . In order to evaluate the prediction accuracy of isothermal models, values of RSS defined in Eq.…”
Section: Resultssupporting
confidence: 67%
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