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Biochemistry (Moscow)

, Volume 75, Issue 9, pp 1160–1164 | Cite as

Enzymes of SPZ7 phage: Isolation and properties

  • P. A. LevashovEmail author
  • D. V. Popov
  • V. M. Popova
  • E. L. Zhilenkov
  • O. A. Morozova
  • N. G. Belogurova
  • S. A. Sedov
  • I. A. Dyatlov
  • N. L. Klyachko
  • A. V. Levashov
Article

Abstract

Bacteriophage enzyme preparations exolysin and endolysin were studied. Exolysin (a phage-associated enzyme) was obtained from tail fraction and endolysin from phage-free cytoplasmic fraction of disintegrated Salmonella enteritidis cells. A new method for purification of these enzymes was developed, and their molecular masses were determined. The main catalytic properties of the studied enzymes (pH optimum and specificity to bacterial substrates) were found to be similar. Both enzymes lyse Escherichia coli cells like chicken egg lysozyme, but more efficiently lyse S. enteritidis cells and cannot lyse Micrococcus luteus, a good substrate for chicken egg lysozyme. Similar properties of exolysin and endolysin suggest that these enzymes are structurally similar or even identical.

Key words

bacteriophage enzyme lysis of bacteria bacteriolytic activity 

Abbreviations

BSA

bovine serum albumin

CFU

colony-forming units

DTT

dithiothreitol

FFH

fish-flour pancreatic hydrolyzate

GPDH

glyceraldehyde-3-phosphate dehydrogenase

PFU

plague-forming units

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References

  1. 1.
    Khalil, R., Frank, J. F., Hassan, A. N., and Omar, S. H. (2006) PNAS, 103, 10765–10770.CrossRefGoogle Scholar
  2. 2.
    Donovan, D. M. (2007) Recent Patents Biotechnol., 1, 113–122.CrossRefGoogle Scholar
  3. 3.
    Rabsch, W., Hargis, B. M., Tsolis, R. M., Kingsley, R. A., Hinz, K.-H., Tschape, H., and Baumler, A. J. (2000) Emerging Infectious Diseases, 6, 443–447.CrossRefPubMedGoogle Scholar
  4. 4.
    Hennessy, T. W., Craig, W., Hedberg, C. W., Slutsker, L., White, K. E., Besser-Wiek, J. M., Moen, M. E., Feldman, J., Coleman, W. W., Edmonson, L. M., MacDonald, K. L., and Osterholm, M. T. (1996) New England J. Med., 334, 1281–1286.CrossRefGoogle Scholar
  5. 5.
    Adams, M. (1961) Bacteriophages [Russian translation], Izd-vo Inostrannoi Literatury, Moscow.Google Scholar
  6. 6.
    Bradford, M. (1976) Analyt. Biochem., 72, 248–254.CrossRefPubMedGoogle Scholar
  7. 7.
    Goa, J. (1953) Clin. Lab. Invest., 5, 218–222.CrossRefGoogle Scholar
  8. 8.
    Levashov, P. A., Sutherland, D. S., Besenbacher, F., and Shipovskov, S. (2009) Analyt. Biochem., 395, 111–112.CrossRefPubMedGoogle Scholar
  9. 9.
    Velick, S. F., and Furfine, C. (1963) Glyceraldehyde 3-Phosphate Dehydrogenase, in The Enzymes (Boyer, P. D., Lardy, H., and Myrback, K., eds.) Vol. 7, 2nd Edn., Academic Press, NY, pp. 243–273.Google Scholar
  10. 10.
    Severin, S. E., and Solov’eva, G. A. (1989) Handbook on Biochemistry [in Russian], Lomonosov Moscow State University, Moscow.Google Scholar
  11. 11.
    Osterman, L. A. (1985) Chromatography of Proteins and Nucleic Acids [in Russian], Nauka, Moscow.Google Scholar
  12. 12.
    Zuev, V. A. (1969) Lytic Activity of Bacterial Viruses [in Russian], Meditsina, Moscow.Google Scholar

Copyright information

© Pleiades Publishing, Ltd. 2010

Authors and Affiliations

  • P. A. Levashov
    • 1
    Email author
  • D. V. Popov
    • 2
  • V. M. Popova
    • 2
  • E. L. Zhilenkov
    • 2
  • O. A. Morozova
    • 3
  • N. G. Belogurova
    • 1
  • S. A. Sedov
    • 1
  • I. A. Dyatlov
    • 2
  • N. L. Klyachko
    • 1
  • A. V. Levashov
    • 1
  1. 1.Faculty of ChemistryLomonosov Moscow State UniversityMoscowRussia
  2. 2.State Research Center for Applied Microbiology and BiotechnologyObolensk, Moscow RegionRussia
  3. 3.Bacteriological Laboratory, Clinical CenterSechenov Moscow Medical AcademyMoscowRussia

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