A recombinant strain for producing human gamma interferon (IFN-γ) E. coli BL 21/pET-IFN-γ was constructed to provide 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 at a level 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 up to 5 mg of the drug from 1 g of wet biomass with a purity of at least 95% and high specific (antiviral) activity.

Here, we performed a comparative evaluation of the effectiveness of the isolation of human interferon-gamma from the biomass of the recombinant strain of E.coli MH-1/pIFN-γ-trp2 enabling constitutive synthesis of the target protein in the "inclusion bodies", and a new recombinant inducible strain of E. coli BL 21/pET-IFN-γ containing the protein in a soluble form. It has been shown that the use of an inducible producer strain can increase the yield of the target protein from 1.5 mg/g to 5 mg/g and enhance the specific (antiviral) activity by 20-fold.

A suggested method for obtaining recombinant human granulocyte-macrophage colony-stimulating factor (GM-CSF) includes the accumulation of the producer strain biomass enriched with the target product up to 30% of total protein content, its isolation and purification. The later consists of the following stages: ultrasound cell disintegration, washing of inclusion bodies with buffer solutions, GM-CSF solubilization from inclusion bodies by 6 M urea, denaturation-renaturation of protein molecules and purification by chromatography on DEAE-Sepharose and combined chromatography on CM-Sepharose and Q-Sepharose followed by dialysis. The proposed method makes it possible to yield up to 10 mg of the protein preparation from 1 g of wet cells with the purity of 98% and high activity shown on the human erythroleukemia cell line. granulocyte-macrophage colony-stimulating, GM-CSF, producer strain, cultivation, chromatographic purification. The work was performed in the framework of the State Assignment «Adjustment of the Technology of Preparative Obtaining and Purification of Recombinant Proteins» (no. 13/18).

Two photosensitizing preparation for the photodynamic therapy of oncological diseases have been obtained. As revealed in this study, under experimental conditions their action suppresses the growth of Enterococcus faecalis and Staphylococcus aureus, which may be of great importance for the treatment of infections. And in contrast to antibiotic therapy, their use may not affect the development of normal intestinal microflora. The study has shown that their derivatives with the residues of carbonic (or muramic) acids more intensively penetrate microorganisms through their cell walls. This makes in possible to expand the spectrum of action of the preparations. The proposed method permits the rapid analysis of the photochemical activity of preparation for photodynamic therapy in the process of their development.