Evaluation of a retention model for high-performance ion-exchange chromatography using two different displacing salts

Influence of pH and Ionic Strength on the Steric Mass-Action Model Parameters around the Isoelectric Point of Protein

“…Such negative charges decrease with decreasing pH, so less and less counterions are displaced during the binding of BSA, and the characteristic charges decrease with pH at pH < 5.5. Similar results for other proteins were also reported by other researchers (19, 24).…”

Influence of pH and Ionic Strength on the Steric Mass-Action Model Parameters around the Isoelectric Point of Protein

“…Such negative charges decrease with decreasing pH, so less and less counterions are displaced during the binding of BSA, and the characteristic charges decrease with pH at pH < 5.5. Similar results for other proteins were also reported by other researchers (19, 24).…”

Prediction of the Effect of Mobile-Phase Salt Type on Protein Retention and Selectivity in Anion Exchange Systems

“…Its retention time decreased when the salt type was changed from NaCl to NaBr, as was the case for several of the proteins; however, its retention time was greater in the presence of Na 2 SO 4 than it was in the presence of NaBrsan observation that was unique for this protein. These results confirm previous results reported in the literature [1][2][3][4][5][6][7] and indicate that the retention of different proteins is altered to various degrees depending on the type of displacing salt type that is employed.…”

Adsorption of Proteins onto Ion-Exchange Chromatographic Media: A Molecular Dynamics Study

“…From the adsorption of bHb it is also indicated that, though the net charge of the total bHb molecule (charge of +2) is akin to that on Q Sepharose FF (positively charged), the bHb surface still has negative charges to interact with the adsorbent. Similar results for other proteins were obtained by experiments. ,, …”

Influence of pH and Ionic Strength on the Steric Mass-Action Model Parameters around the Isoelectric Point of Protein

“…Such negative charges decrease with decreasing pH, so less and less counterions are displaced during the binding of BSA, and the characteristic charges decrease with pH at pH < 5.5. Similar results for other proteins were also reported by other researchers (19, 24).…”

Prediction of the Effect of Mobile-Phase Salt Type on Protein Retention and Selectivity in Anion Exchange Systems

“…Its retention time decreased when the salt type was changed from NaCl to NaBr, as was the case for several of the proteins; however, its retention time was greater in the presence of Na 2 SO 4 than it was in the presence of NaBrsan observation that was unique for this protein. These results confirm previous results reported in the literature [1][2][3][4][5][6][7] and indicate that the retention of different proteins is altered to various degrees depending on the type of displacing salt type that is employed.…”

Adsorption of Proteins onto Ion-Exchange Chromatographic Media: A Molecular Dynamics Study

“…From the adsorption of bHb it is also indicated that, though the net charge of the total bHb molecule (charge of +2) is akin to that on Q Sepharose FF (positively charged), the bHb surface still has negative charges to interact with the adsorbent. Similar results for other proteins were obtained by experiments. ,, …”

Influence of pH and Ionic Strength on the Steric Mass-Action Model Parameters around the Isoelectric Point of Protein

“…Such negative charges decrease with decreasing pH, so less and less counterions are displaced during the binding of BSA, and the characteristic charges decrease with pH at pH < 5.5. Similar results for other proteins were also reported by other researchers (19, 24).…”

Prediction of the Effect of Mobile-Phase Salt Type on Protein Retention and Selectivity in Anion Exchange Systems

“…Its retention time decreased when the salt type was changed from NaCl to NaBr, as was the case for several of the proteins; however, its retention time was greater in the presence of Na 2 SO 4 than it was in the presence of NaBrsan observation that was unique for this protein. These results confirm previous results reported in the literature [1][2][3][4][5][6][7] and indicate that the retention of different proteins is altered to various degrees depending on the type of displacing salt type that is employed.…”

Adsorption of Proteins onto Ion-Exchange Chromatographic Media: A Molecular Dynamics Study

“…From the adsorption of bHb it is also indicated that, though the net charge of the total bHb molecule (charge of +2) is akin to that on Q Sepharose FF (positively charged), the bHb surface still has negative charges to interact with the adsorbent. Similar results for other proteins were obtained by experiments. ,, …”