PURIFICATION OF RECOMBINANT EEL GROWTH-HORMONE

A purification procedure for highly purified and highly uniform recombinant eel growth hormone (EGH) was established and found to be applicable to large-scale production. Inclusion bodies of recombinant EGH expressed in Escherichia coli were obtained by the disruption of cells and washing. The inclusion bodies were solubilized in urea solution and refolded by dilution and addition of oxidized glutathione. EGH analogues such as oxidized EGH at methionine and formylated EGH at N-terminal, which were produced during the fermentation and/or purification process, were removed by subsequent hydrophobic interaction chromatography.