Capillary electrophoresis of recombinant proteins

1997 
Many naturally occurring proteins which are used therapeutically have been cloned and expressed in large quantities in bacterial, yeast or mammalian systems. Purification of these proteins by column chromatography generates high purity products with low levels of host protein contaminants. However, isoforms of the desired protein may be present at variable concentrations. Analysis of these variant forms has been enhanced by the utilisation of capillary electrophoresis (CE), a highly efficient, widely applicable technique which is increasingly used in the field of biotechnology. The role of CE in the analysis of recombinant proteins is reviewed with respect to microcharacterisation, comparison of natural and recombinant proteins, separation of mutant or variant forms and analysis of glycoforms. Examples of these applications are described and illustrated with analysis of recombinant human albumin. The rapid development of CE, further enhancing its versatility, and its use with complementary analytical techniques is also discussed.
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