FIELD: biochemistry, biotechnology, medicine. SUBSTANCE: human recombinant granulocytic colony-stimulating factor is prepared from Escherichia coli transformed cells. Inclusion bodies comprising recombinant factor are dissolved in urea and reduction reaction is carried out with 10 mM of 2-mercaptoethanol. Renaturation is carried out by addition of EDTA-containing neutral buffer up to 0.8 M concentration of urea. Chromatography purification of recombinant factor is carried out on two successively linked columns filled with DEAE-cellulose and SP-Sephadex and the following elution of the end protein from SP-Sephadex column by linear gradient of sodium chloride in 0.02 M sodium acetate buffer, pH 4.4-4.5. Invention provides to increase the yield of product and retain its biological activity and purity. Invention can be used for isolation and purification of physiologically active human recombinant granulocytic colony-stimulating factor. EFFECT: improved method of preparing, increased yield and purity. 2 cl, 3 tbl, 3 dwg
