Separation of recombinant porcine growth hormone monomer from dimer and other oligomers in the production process from E. coli inclusion bodies

Abstract

Porcine growth hormone expressed in E. coli accumulates as inclusion bodies. After the refolding process, besides the monomer, also a dimer and higher oligomers of this protein were found. A successful application of hydrophobic chromatography for porcine growth hormone monomer separation from other forms in the production process is described. The results of target protein purification from 4 g of biomass are presented. Keywords: porcine growth hormone, hydrophobic chromatography, inclusion bodies, aggregation