Abstract: 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.

Abstract: Purification and activation of proteins produced in transformant microorganisms as insoluble, biologically inactive inclusion bodies can be effected by solubilizing the inclusion bodies in SDS; dialyzing or refrigerating the protein solution to remove a portion of the SDS; chromatographing the protein solution on an ion-retardation resin to remove the remaining SDS from the protein; and chromatographing the protein solution thus obtained on an anion-exchange resin.