EFFECT OF ARGININE ON GLYCATION AND STABILITY OF RECOMBINANT HUMAN INTERFERON-GAMMA

摘要

Recombinant human interferon-gamma (rhIFN-y) produced in Escherichia coli (E. coli) undergoes structural and functional alterations as a result of two different but parallel processes - aggregation and non-enzymatic glycosylation (gly cation). Findingapproaches for their inhibition is of great importance for the quality of the rhIFN-gamma. In this study we used arginine for this purpose. We found that arginine added to the E. coli culture medium, inhibits formation of fluorescent gly cation adductsand imidazolone in the total bacterial protein but does not interfere with the early gly cation stages. In addition, refolding and storage of rhlFN-gamma in the presence of arginine led to delayed accumulation of N-(carboxymethyl)lysine and structural stabilization of the recombinant protein.