PURIFICATION OF RECOMBINANT HUMAN COLLAGEN-LIKE BIOPROTEIN II BY ION EXCHANGE CHROMATOGRAPHY

A purification method of recombinant human collagen-like Bioprotein II(HCB II) by the CM52 cation exchange chromatography were reported.The batch operation and normal chromatography column method were used in experiments,i.e.,Batch operation of chromatography: HCB II was absorbed under pH 4.0,NaCl(ionic strength) 0.15mol/L,17.26ml(protein volume)/g(resin) and concentration of crude protein liquid 7g/L;Column chromatography: HCB II was absorbed under pH 4.0,NaCl(ionic strength) 0.15mol/L,flow rate 5ml/min and concentration of crude protein liquid 5g/L,the elution of HCB II was pH 4.0,the concentration of NaCl(ionic strength) 0.30mol/L.As a result,the CM52 cation exchange chromatography was of better capacity of adsorption for HCBⅡ and the elution was simple;the total purity process time would be shorten and resolution was high,The recovery of aim protein HCB II with a molecular weight around 97kD was above 83.8% and purity of HCB II could reach electrophoresis grade purity.