PURIFICATION OF RECOMBINANT HUMAN INTERFE RON-GAMMA BY HIGH-PERFORMANCE HYDROPHOBIC INTERACTION CHROMATOGRAPHY AND SIZE-EXCLUSION CHROMATOGRAPHY

A downstream purification procedure for recombinant human interferon-g amma(rhIFN-gamma) expressed in E. coli was described. An essentially t wo-step chromatographic purification procedure, i. e., size exclusion chromatography (SEC) and high-performance hydrophobic interaction chro matography (HPHIC), was used for purification of homogeneity of rhIFN- gamma from the inclusion body. The specific activity of purified rhIFN -gamma was 1.0 X 10(8) IU/mg protein. The product of purification rhIF N-gamma was analyzed by an analytical high-performance SEC and a signi ficant sigle symmetrical peak had been found. The purity of purified r hIFN-gamma was greater than 95% from analysis, determination by analyt ical HPSEC and SDS-PAGE with Coomssie Blue. The molecular weight was c a. 15 000. It was shown that this procedure was an effective method fo r purifying rhIFN-gamma.