Affinity Chromatographic Purification of Proteins Using Immobilized Cells

Abstract

Affinity chromatography has over the last ten years developed from being a research instrument to becoming a routinely used method. A leading theme during these developments ahs been to use affinity sorbents, which from a chemical point of view, were well-defined and offered few possibilities for unspecific interactions. However, some ligands may be too complicated or too expensive tc synthesize in order to be used as affinity ligands. Therefore, a recent development in affinity chromatography has dealt with the use of immobilized whole cells as affinity supports and surface structures on these immobilized cells have been used as ligands. Recently, cells cross linked by glutaraldehyde and mixed with Sephadex G-25 have been used in lectin purification (1). The use of cells adsorbed to ion-exchangers as affinity systems has also been described (2), but serious leakage of cells from the support took place during the affinity chromatographic procedure.