Зинченко Алексей Алексеевич

Кандидат химических наук

Старший научный сотрудник (Лаборатория биотехнологии)

Тел.: +7 (903) 7096928

Эл. почта: alezina@mail.ru


Период обученияСтрана, городУчебное заведениеДополнительная информация
1968–1973 СССР, РСФСР, Казань Казанский государственный университет им. В.И. Ульянова-Ленина. Химический факультет

Премии и заслуги

Премия Правительства Российской Федерации в области науки и техники за создание производства и внедрение в практику отечественного здравоохранения генно-инженерного инсулина человека.Постановление Правительства РФ от 20 февраля 2006 г. Диплом лауреата №6863.

Избранные публикации

  1. Kotelnikova O.V., Zinchenko A.A., Vikhrov A.A., Alliluev A.P., Serova O.V., Gordeeva E.A., Zhigis L.S., Zueva V.S., Razgulyaeva O.A., Melikhova T.D., Nokel E.A., Drozhzhina E.Y., Rumsh L.D. (2016). Serological Analysis of Immunogenic Properties of Recombinant Meningococcus IgA1 Protease-Based Proteins. Bull. Exp. Biol. Med. 161 (3), 391–4 [+]
  2. Zhigis L.S., Kotelnikova O.V., Vikhrov A.A., Zinchenko A.A., Serova O.V., Zueva V.S., Razgulyaeva O.A., Gordeeva E.A., Melikhova T.D., Nokel E.A., Alliluev A.P., Drozhzhina E.Y., Rumsh L.D. (2015). A new methodological approach to estimation of IgA1 and IgA2 content in human serum using recombinant IgA1 protease from Neisseria meningitidis. Biotechnol. Lett. 37 (11), 2289–93 [+]

    A new approach to estimation of IgA subclass levels and IgA1/IgA2 ratio using enzymatically active and inactive forms of Neisseria meningitidis IgA1 protease was developed.

  3. Mikhailova A.G., Nekrasov A.N., Zinchenko A.A., Rakitina T.V., Korzhenevsky D.A., Lipkin A.V., Razguljaeva O.A., Ovchinnikova M.V., Gorlenko V.A., Rumsh L.D. (2015). Truncated Variants of Serratia proteamaculans Oligopeptidase B Having Different Activities. Biochemistry Mosc. 80 (10), 1331–43 [+]

    Treatment of native psychrophilic oligopeptidase B from Serratia proteamaculans (PSP, 78 kDa) with chymotrypsin (soluble or immobilized on modified porous glass MPG-PA) in the presence of 50% glycerol leads to production of a truncated enzyme form (PSP-Chtr, ~66 kDa), which retains activity toward the low molecular weight substrate of PSP, BAPNA, but in contrast to PSP, is active toward the protein substrate azocasein. It has been shown by MALDI-TOF mass-spectrometry that PSP-Chtr lacks the N-terminal region of the molecule that envelops the catalytic domain of PSP and supposedly prevents hydrolysis of high molecular weight substrates. It has also been established that the lacking fragment corresponds to the N-terminal highest rank element of the informational structure of PSP. This finding confirms the usefulness of the method of informational structure analysis for protein engineering of enzymes. A similar treatment of PSP with immobilized trypsin also led to production of a stable truncated enzyme form (PSP-Tr, ~75 kDa) which lacked 22 C-terminal amino acid residues and completely lost enzymatic activity, presumably because of changes in the nearest environment of His652 of the catalytic triad.

  4. Zinchenko A.A., Alliluev A.P., Serova O.P., Gordeeva E.A., Zhigis L.S., Zueva V.S., Razgulyaeva O.A., Melikhova T.D., Nokel E.A., Drozhzhina E.Y.u., Kotelnikova O.V., Rumsh L.D. (2015). Immunogenic and protective properties recombinant proteins based on meningococcal IgA1 protease. J Meningitis 1 (102), [+]

    Recombinant proteins (M1K2–N963-LEH6, MA28–N963-LEH6 and ME135–H328-LEH6) have been created on the basis of the genome sequence of IgA1 protease of N. meningitidis serogroup B strain H44/76. It is revealed that, similarly to the native enzyme isolated earlier from N. meningitidis serogroup A strain A208, these proteins induce formation of animal protection against the infection with the virulent strain of meningococcus serogroup B. It is shown that these compounds are promising as a basis for a polyvalent anti-meningococcal vaccine.

  5. Kotelnikova O.V., Alliluev A.P., Drozhzhina E.I.u., Koroleva I.S., Sitnikova E.A., Zinchenko A.A., Gordeeva E.A., Melikhova T.D., Nokel E.A., Zhigis L.S., Zueva V.S., Razguliaeva O.A., Serova O.V., Iagudaeva E.I.u., Rumsh L.D. (2014). [Protective properties of recombinant IgA1 protease from meningococcus]. Biomed Khim 60 (4), 479–86 [+]
  6. Nekrasov A.N., Zinchenko A.A. (2010). Structural features of the interfaces in enzyme-inhibitor complexes. J. Biomol. Struct. Dyn. 28 (1), 85–96 [+]
  7. Liubavina I.A., Zinchenko A.A., Salomatina I.S., Zherdev A.V., Dzantiev B.B. (2009). [Immunochromatographic analysis of 2,4-dichlorophenoxyacetic acid and simazine using monoclonal antibodies labelled with colloidal gold]. Bioorg. Khim. 30 (2), 201–7 [+]
  8. Liubavina I.A., Zinchenko A.A., Lebedin Iu.S., Chukanov S.V. (2009). [Development of a rapid method for the detection of prostate-specific antigen by immunochromatography]. Bioorg. Khim. 33 (5), 550–4 [+]
  9. Nekrasov A.N., Zinchenko A.A. (2008). Hydrolases: the correlation between informational structure and the catalytic sites organization. J. Biomol. Struct. Dyn. 25 (5), 553–61 [+]
  10. Shoibonov B.B., Osipov A.V., Kryukova E.V., Zinchenko A.A., Lakhtin V.M., Tsetlin V.I., Utkin Y.N. (2005). Oxiagin from the Naja oxiana cobra venom is the first reprolysin inhibiting the classical pathway of complement. Mol. Immunol. 42 (10), 1141–53 [+]
  11. Vorobjeva L., Leverrier P., Zinchenko A., Boyaval P., Khodjaev E., Varioukhina S., Ponomareva G., Gordeeva E., Jan G. (2004). Anti-stress activity of Propionibacterium freudenreichii : identification of a reactivative protein. Antonie Van Leeuwenhoek 85 (1), 53–62 [+]Propionibacterium freudenreichii subsp. shermanii is known to prevent mutations caused by various agents such as N-methyl-N'-nitro-N-nitrosoguanidine, 9-aminoacridine, 4-nitro-quinoline-1-oxide and by UV radiation in both prokaryotic and eukaryotic cells. It was also shown to prevent or repair damage caused by H(2)O(2) or UV radiation in Salmonella typhimurium and Escherichia coli, a characteristic previously designated as reactivative effect. In order to characterise this effect at the molecular level, we have purified the active component from a P. freudenreichii cell-free extract using a combination of ammonium sulfate precipitation, anion-exchange and size-exclusion chromatography. The isolated 35 kDa protein was then identified using both N-terminal and internal peptide sequencing as a cysteine synthase. The latter was localised in the P. freudenreichii proteomic map. It is constitutively expressed but also clearly induced during adaptation to detergent and heat, but not acid, stresses. The biological meaning of cysteine synthase in the context of adaptation to oxidative and non-oxidative stresses is discussed. ID:1656
  12. Liubavina I.A., Salomatina I.S., Zinchenko A.A., Zherdeev A.V., Dzantiev B.B. (2000). [A noninstrumental Immunoassay based on colloidal dyes]. Bioorg. Khim. 26 (3), 231–7 [+]
  13. Pavlova I.S., Lyubavina I.A., Zherdev A.V., Zinchenko A.A. (1997). [Simple immunoassays of pesticides based on the biotin-streptavidin system]. Bioorg. Khim. 23 (10), 832–8 [+]
  14. Dergousova N.I., Leonova Yu.F., Zinchenko A.A., Rumsh L.D., Andreeva N.S. (1997). MUTANT OF HIV-1 PROTEASE WITH NEW SPECIFIC PROPERTIES. Protein Pept. Lett. 4 (5), 321–328 [+]
  15. Voitenko V.G., Bayramashvili D.I., Zebrev A.I., Zinchenko A.A. (1990). Relationship between structure and histamine releasing action of polymyxin B and its analogues. Agents Actions 30 (1-2), 153–6 [+]
  16. Trakhanova M.N., Zinchenko A.A., Okhanov V.V., Dubovskii P.V., Bairamashvili D.I. (1989). [Structural and functional investigation of polymyxins. Structure and biological properties of polymyxin M analogs]. Antibiot. Khimioter. 34 (1), 20–4 [+]
  17. Bairamashvili D.I., Zinchenko A.A., Maslin D.N., Trakhanova M.N., Miroshnikov A.I. (1988). [The action of combinations of the nonapeptide polymyxin B with antibiotics on gram-negative bacteria]. Antibiot. Khimioter. 33 (8), 591–4 [+]
  18. Trakhanova M.N., Zinchenko A.A., Bairamashvili D.I., Makarova R.A., Samoĭlova L.N. (1988). [Structural and functional study of polymyxins. Isolation and properties of individual components of polymyxin M]. Antibiot. Khimioter. 33 (4), 262–6 [+]
  19. Okhanov V.V., Dubovskii P.V., Trakhanova M.N., Bairamashvili D.I., Zinchenko A.A. (1987). [Structural and functional research on polymyxins. 1H NMR analysis of the conformation of polymyxin M in water]. Antibiot. Med. Biotekhnol. 32 (10), 738–43 [+]
  20. Kozlov L.V., Shibanova E.D., Zinchenko A.A. (1987). [Formation of classical C3 convertase during the alternative pathway of human complement activation]. Biokhimiia 52 (4), 660–6 [+]
  21. Kozlov L.V., Sizoĭ M.N., Zinchenko A.A., Levkovskiĭ A.V. (1986). [Inhibition of the binding and activation of the first component of human complement. The effect of synthetic peptides, immunoglobulin fragments and various proteins]. Biokhimiia 51 (5), 707–18 [+]
  22. Tétin S.I.u., Efetov K.A., Troitskiĭ G.V., Kozlov L.V., Zinchenko A.A. (1985). [Complement fixation activity of immunoglobulin G in ethylene glycol solutions]. Bioorg. Khim. 11 (8), 1068–73 [+]
  23. Kozlov L.V., Zinchenko A.A., Sizoĭ M.N., Kretova A.F., Tikhonenko A.S. (1985). [Changes in the ultrastructure of subcomponent C1q of human complement during spontaneous inactivation in diluted solutions]. Bioorg. Khim. 11 (1), 37–42 [+]
  24. Kozlov L.V., Sizoĭ M.N., Zinchenko A.A., Ivanov A.E., Zubov V.P. (1984). [Binding and activation of the first component of human complement on artificial matrices]. Bioorg. Khim. 10 (12), 1629–38 [+]
  25. Kozlov L.V., Soliakov L.S., Zinchenko A.A. (1984). [A new low molecular-weight protein effector of human complement from the venom of the Central Asian cobra Naja naja oxiana]. Bioorg. Khim. 10 (3), 323–32 [+]
  26. Kozlov L.V., Zinchenko A.A., Soliakov L.S., Sizoĭ M.N., Ishchenko A.M. (1983). [A mechanism of human complement activation by immunostimulators from the bacterial cell wall]. Bioorg. Khim. 9 (8), 1047–55 [+]
  27. Антонов В.К., Зинченко А.А., Румш Л.Д. (1976). Статистический анализ специфичности пепсина в отношении гидролиза белков. Биоорг. хим. 2 (6), 803–810 ID:253