| 摘要 |
Purification and solubilization of proteins produced in transformant microorganisms as insoluble, biologically inactive inclusion bodies is effected by solubilizing the inclusion bodies in SDS; treating the SDS-protein solution with urea; removing the SDS and purifying the protein by chromatography on an anion-exchange resin having cationic groups attached to a polysaccharide support; and dialyzing the solution obtained from the anion-exchange resin to remove urea, thereby allowing the protein to fold into its native conformation. The solution thus obtained can be activated by removing soluble protein aggregates via ultrafiltration or chromatography on a weak anion-exchange column. |
