원문정보
초록
영어
Recombinant protein produced by E. coli often expressed as inclusion bodies (IBs). To convert these IBs into active forms, protein refolding process is needed. Recently, hydrophobic interaction chromatography (HIC) has been introduced as one of the potential process for protein refolding since hydrophobic interaction is the dominant force in protein folding and structure stabilization.1) HIC can be an artificial chaperone system through its interaction among
denatured protein, hydrophobic ligands and denaturant. Guanidine hydrochloride, as a denaturant, is known to be applied directly into HIC column without any damages on protein structures. Moreover, removal of impure proteins from IBs during refolding procedures is another advantage of chromatography-based refolding methods. In this study, Interferon alpha 1 (IFNα1) was selected since it is a well-known therapeutic protein for virus infection and cancers and highly expressed IFNα1 frequently forms IBs. IFNα1 has been studied for treatment of
various viral diseases such as hepatic fibrosis caused by hepatitis B, herpes simplex virus keratitis, and bovine respiratory diseases in calves.2) Treatment procedures using various HIC resins were developed for the refolding of IFNα1.