The synthesis of packing of oxygen-ethane as end-ligand bonded to silica andseparation for recombinant human interferons(rhIFN) in high-performance hydrophobicinteraction chromatography has been studied in this paper. It was showed that the packingsynthesized was not only suitable for separating standard proteins, but also for different rhIFNs,i. e., rhIFN-αA expressed in yeast, rhIFN-αA and rh1FN-γ in E. colt. The purify of threerhIFNs purified by one-step HPHIC, which rhIFN-γ expressed in E. colt was recognized as80%, rhIFN-αA expressed in yeast as 70%, and rhIFN-αA expressed in E. colt as 30%, wasmore than that of other chromatography besides affinity chromatography.
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