Abstract
A recombinant strain producing human gamma interferon (IFN-γ) E. coli BL 21/pET-IFN-γ was constructed, providing a high level of its expression. A method has been developed for obtaining a soluble form of recombinant IFN-γ, consisting of the processes of producing a biomass of a producer strain containing a target protein in an amount of 32–37% of the total content of cellular proteins, protein isolation and purification. The purification process included the stages of disintegration, clarification of the cell lysate, chromatographic purification and dialysis. The developed method makes it possible to obtain from 1 g of wet biomass up to 5 mg of the drug with a purity of at least 95% and high specific (antiviral) activity.
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