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[Study on protein separation using immobilized metal ion affinity chromatography].

Immobilized metal ion affinity chromatography (IMAC) has shown promise of isolating desired proteins from a mixture based on their difference of affinity for chelated metal ions. With its technological superiority, such as large adsorption capacity, mild separation condition, simple ligands and wide applications, IMAC has become powerful tool for biotechnological products separation, such as proteins, amino acids and gene products. In spite of many sophisticated applications for IMAC, the theoretical analysis of Immobilized metal chromatography has remained insufficient. In this paper, the eluted efficiencies of bovine serum albumin (BSA) in a single-component system under different elution conditions are studied. The effects of several elution factors, such as pH value, ammonium concentration and anion species on protein separation are studied. Comparing the elution data of BSA in IDA-Cu and IDA-Zn columns, the different ability of affinity between metal ions and proteins is found. In addition, the elution behaviors of different proteins are investigated. This work facilitates the further research in separation of real systems.