A simple, selective and high capacity process is described for the preparative purification of recombinant human insulin A chain, using ion exchange chromatography. This process was developed considering the particular physicochemical characteristics of this peptide. We have found that the insulin A chain binds strongly to the anionic exchanger Macro Prep 50 Q, which permits the equilibration of the resin to an ionic strength of 0.5 M NaCl. These conditions avoid the adsorption of most contaminant components, thus incrementing the capacity of the support for the insulin A chain. Moreover, the process can be easily automatized and scaled-up.
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