Production, purification and characterization of recombinant human interferon γ

Expression of Recombinant Human Interferon-γ with Antiviral Activity in the Bi-Cistronic Baculovirus-Insect/Larval System

“…The amount of the purified recombinant hIFN-(39 mg, 46.5% of total protein) from the serum-free medium acquired in this study is as good as the yields reported when hIFN-was expressed in different systems, as in the E. coli, where 32% purified bioactive hIFN-was recovered, 44) and the high density cultivation technique due to Khalilzadeh and co-workers 15) where 0:35 AE 0:02 g, rhIFN-/g, dry E. coli cell weight was generated. About 699.79 ng/g, cells of secretory and intracellular bioactive human interferon gamma against dengue virus rhIFN-was obtained from transgenic rice suspension cells.…”

Increased yield of high purity recombinant human interferon-γ utilizing reversed phase column chromatography

“…In the food and animal industries, IFN-γ is effective against a variety of economically important animal viral diseases [16,17]. Hence, the commercial interests in efficiently optimizing the production yields and specific activities of IFN-γ preparations are tremendous [18][19][20][21][22].…”

Glycation and Post-translational Processing of Human Interferon-γ Expressed in Escherichia coli

“…Partial proteolysis yielding at least three truncated species further contributes to protein microheterogeneity (14 -16). Extensive experimental evidence indicates that cleavage of rhIFN-␥ occurs at its C terminus adjacent to basic amino acids (17)(18)(19). Proteolysis of rhIFN-␥ is usually attributed to specific (trypsin-like) proteases; however, it is observed also in purified protein samples either stored in solution (18,20) or lyophilized (21).…”