Abstract
Protein variants and isoforms were successfully separated on MCI GEL ProtEx ion-exchange HPLC columns. There was no irreversible adsorption of proteins, and sample proteins were quantitatively recovered. Species variants of cytochrome c (bovine, horse and rabbit) were completely separated on a sulfopropyl (ProtEx-SP) stationary phase in a gradient system. Diethylaminoethyl (ProtEx-DEAE) phase was determined to be effective for the separation of human growth hormone and its deamidated isoforms. These characteristics of ProtEx stationary phases may be attributed both to particle uniformity and to hydrophillic surface coverage of the base polymeric material.
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