Purification Of Recombinant Human-like Collagen Bioprotein Ⅱ By Ion Exchange Chromatography

Ion exchange chromatography with low cost, was used to purify Human-like Collagen Bioprotein â…¡ (HCB â…¡) , harvested recombinant E.coli cell was lysed by high pressure homogenizer, supernatant was collected by centrifuging. After salt precipitation, the crude product solution of HCB II was purified with ion exchange chromatography, the purity of HCB II could reach electrophoresis grade purity.Cation exchange resin CM52 was suitable for the purification of HCB II than the other five kind resins used in the experiment. The CM52 cation exchange resin was of better capacity of adsorption and selectivity for HCB â…¡. Under the conditon of pH 4.0, buffer free of NaCl, the adsorption capacity of CM52 for HCBâ…¡ was 54.8mg/g.wet resin and seperation factor was 2.64.The experiments of adsorption equilibrium showed that the adsorption of HCB II onto CM52 obeyed Langmuir model. Ionic strength and pH value were two important factors affecting the equilibrium characteristics. The model parameters hardly vary with pH value unless pH