Abstract
ABSTRACTRecombinant human interferon-gamma (rhIFN-γ) 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 (glycation). Finding approaches for their inhibition is of great importance for the quality of the rhIFN-γ. In this study we used arginine for this purpose. We found that arginine added to the E. coli culture medium, inhibits formation of fluorescent glycation adducts and imidazolone in the total bacterial protein but does not interfere with the early glycation stages. In addition, refolding and storage of rhIFN-γ in the presence of arginine led to delayed accumulation of Nε-(carboxymethyl)lysine and structural stabilization of the recombinant protein.
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