Abstract
The addition of neutral water-soluble polymers such as polyethylene glycol to the eluent of standard ion-exchange chromatography systems affects the separations of proteins in a useful and predictable manner. The relative effects of various polymers are predictable on the basis of their hydrophobicities. Protein retention times are increased, especially for larger and/or more hydrophobic proteins, as predicted by the same order as protein precipitation by neutral polymers. Therefore, this “polymer enhanced chromatography” technique can be particularly useful for the separation of proteins or other biopolymers with the same isoelectric points but different sizes. Examples would include the separation of monomers from dimers and higher order aggregates, or of intact proteins from fragments. Examples of applications with model proteins and the separation of bovine somatotropin monomer and dimer are presented.
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