Prediction of Protein Retention Times in Anion-Exchange Chromatography Systems

Abstract

INTRODUCTION Ion-Exchange Chromatography (IEC) is a widely accepted standard bioseparation technique that has been growing in importance during the past decade in keeping with current rapid developments in biotechnology. To date, there are two main kinds of IEC: cation-exchange and anion-exchange chromatography, determined by whether a negative charge (cation-exchange) or a positive charge (anion-exchange) is carried by the functional groups on the surface of the IEC stationary phase. The ionic biopolymers, such as proteins, are separated primarily through the electrostatics interactions between the charged surface of the ion-exchange resin and the ionic solutes bearing the opposite charge. In the case of anion-exchange chromatography, negatively charged proteins bind in a transient fashion to the positively charged stationary phase sites, as long as the salt concentration is kept low. Proteins bound with different degrees of interaction can be separated with the aid of an increasin