Refolding of ten denatured standard proteins by high performance hydrophobic interaction chromatography

    HUANG Yaª²Yu1,TONG Wei2,GUO Liª²An3

    1Department of Hematology,Xijing Hospital,2Dean¡¯s Office,3Department of Chemistry,School of Basic Medicine,Fourth Military Medical University,Xi¡¯an 710033,China

    ¡¾Abstract¡¿ AIM£º To investigate the refolding of the denatured proteins by high performance hydrophobic interaction chromatography(HPHIC).METHODS£º Ten standard proteins were denatured by guanidine hydrochloride and urea or sodium dodecyl sulfate,and then were refolded by HPHIC in the mobile phrase of (NH4) 2SO4.The retention time,Z value,mass and bioactivity recovery were detected.RESULTS£º Among the ten denatured proteins,five proteins were refolded by HPHIC,in which lysozyme and ribonuclease had high mass and bioactivity recovery and their retention time,peak form and Z value were identical with those of the respective natural proteins.CONCLUSION£º HPHIC has the advantage of good renaturation efficiency. ......