Феофанов Сергей Анатольевич

Избранные публикации

  1. Таран С.А., Верёвкина К.Н., Феофанов С.А., Мирошников А.И. (2009). Ферментативное трансгликозилирование природных и модифицированных нуклеозидов иммобилизованными термостабильными нуклеозидфосфорилазами из Geobacillus stearothermophilus. Биоорг. хим. 35 (6), 822–829 ID:198
  2. Romanov V.P., Bezuglov V.V., Bobrov M.I.u., Kostromina T.I., Feofanov S.A., Miroshnikov A.I. (2009). [Isolation of expressed in E. coli human interferon beta1b (Ser17) by ion-exchange chromatography]. Bioorg. Khim. 37 (3), 327–33 [+]

    A method for isolation of interferon beta1b (Serl7) from inclusion bodies, comprising the steps of solution and reduction of protein from the inclusion bodies, refolding, chromatography on DEAE-Sepharose, chromatography on SP-Sepharose, concentrating, desalting and addition of stabilizers. The solution of reduced protein was diluted with pH 8.0 buffer of 50 mM Tris-HCl, 25 microM CuCl2 and 0.5% Twin 20 for refolding. We used gradient of pH (from 9.3 upto 11.3) for elution of interferon-beta from cation-exchange column. We concentrated of eluate and then desalted on the Sephadex G-50 column with 1 mM NaOH. Then the protein solution was neutralized with mannitol and Na-phosphate. Obtained preparation of interferon-beta was pure by gel-electrophoresis and by HPLC analysis, and had practically indentical level of antiproliferative activity with well-known preparation of Betaferone. Thus we show the possibility of isolation and obtaining of pure and active interferone-beta by ion-exchange chromatography in the presence of non-ion detergent Twin 20. We believe this method for interferon betalb preparation is perspective for scaling and using in the develop of industrial technology for production of this preparation.

    ID:581
  3. Mikoulinskaia G.V., Gubanov S.I., Zimin A.A., Kolesnikov I.V., Feofanov S.A., Miroshnikov A.I. (2003). Purification and characterization of the deoxynucleoside monophosphate kinase of bacteriophage T5. Protein Expr. Purif. 27 (2), 195–201 [+]

    Deoxynucleoside monophosphate kinase (dNMP kinase) of bacteriophage T5 (EC 2.7.4.13) was purified to apparent homogeneity from phage-infected Escherichia coli cells. Electrophoresis in sodium dodecyl sulfate-polyacrylamide gel showed that the enzyme has a molecular mass of about 29 kDa. The molecular mass of dNMP kinase estimated by analytical equilibrium ultracentrifugation turned out to be 29.14 +/- 3.03 kDa. These data suggest that the enzyme exists in solution as a monomer. The isoelectric point of dNMP kinase was found to be 4.2. The N-terminal amino acid sequence, comprising 21 amino acids, was determined to be VLVGLHGEAGSGKDGVAKLII. A comparison of this amino acid sequence and those of known enzymes with a similar function suggests the presence of a nucleotide-binding site in the sequenced region.

    ID:202