A new chromatographic method for fast separation of active proteins

A new method with only a single chromatographic column to accomplish the separation of intact protein molecules by the combination of ion exchange chromatography and hydrophobic interaction chromatography is firstly presented. By selecting twice a suitable stationary phase, mobile phase, buffer exchange condition, and sample injection, some proteins usually required to separate with two-dimensional chromatography can now be accomplished only using the single column in one hour. In addition, the separated proteins can maintain their original three-or four-dimensional molecular structure. It would be expected that this method can also provide a new thought for sample pre-frac-tionation in proteomic investigation, especially, for the limitation of sample source.