Title of article
Modelling oligomer formation in chromatographic separations
Author/Authors
Mollerup، نويسنده , , Jّrgen M.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2011
Pages
5
From page
8869
To page
8873
Abstract
Oligomer forms of proteins are formed by self and cross association or complex formation with ligands. Modelling studies using an ion-exchange adsorbent have demonstrated that the formation of an oligomer form of a target protein can improve a chromatographic separation because the oligomer form displaces the impurities. The results of the investigation show that the process is very robust, that the purity, the yield, and the productivity increase with increasing load and increasing salt concentration in the eluant. An impurity level less than 1 ppm is easy to achieve having a yield of 98%. A universal model for the adsorption equilibria of mono and oligomer forms of proteins on ion-exchange, hydrophobic, and bimodal adsorbents has been developed.
Keywords
Oligomer formation , Preparative ion-exchange chromatography , Preparative displacement chromatography , bimodal , Adsorption isotherms , Quality by design , Process design simulations , Mixed mode
Journal title
Journal of Chromatography A
Serial Year
2011
Journal title
Journal of Chromatography A
Record number
1514727
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