Advertisement

Biophysics

, Volume 53, Issue 4, pp 286–289 | Cite as

Tryptophan phosphorescence study of the influence of detergents on the internal dynamics of human erythrocyte membrane proteins

  • V. M. Mazhul’
  • I. V. Galets
Cell Biophysics
  • 37 Downloads

Abstract

Room-temperature tryptophan phosphorescence was used to assess the slow (millisecond) internal dynamics of proteins in isolated human erythrocyte membranes under the action of detergents: dodecylsulfate, lauroyl sarcosinate, deoxycholate, digitonin, and Tween 20 (concentrations varied from 0.01 to 6 mM). All detergents markedly enhanced the slow internal dynamics, but the dose-response patterns were specific for each agent. The aggregate data support the idea that the slow internal dynamics is restricted in membrane proteins relative to soluble proteins mostly because of intramembrane protein association and isolation from the aqueous milieu, with a possible contribution of a more rigid secondary structure.

Key words

room-temperature tryptophan phosphorescence protein internal dynamics human erythrocyte membranes detergents 

Abbreviations

dCh

deoxycholate

LS

lauroyl sarcosinate

RTTP

room-temperature tryptophan phosphorescence

SID

slow internal dynamics. Deceased

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    S. V. Konev, Structural Lability of Biological Membranes and Regulatory Processes (Nauka i Tekhnika, Minsk, 1987) [in Russian].Google Scholar
  2. 2.
    V. M. Mazhul’, E. M. Zaitseva, and D. G. Shcherbin, Biofizika 45, 965 (2000).Google Scholar
  3. 3.
    V. M. Mazhul’, E. M. Zaitseva, and D. G. Shcherbin, Vestsi NAN Belarusi no. 4, 124 (2000).Google Scholar
  4. 4.
    V. M. Mazhul’, Yu. S. Ermolaev, V. A. Bobrov, et al., Vestsi AN BSSR Ser. Biol. Navuk no. 6, 52 (1976).Google Scholar
  5. 5.
    V. M. Mazhul’, S. V. Konev, Yu. S. Ermolaev, et al., Biofizika 28, 980 (1983).Google Scholar
  6. 6.
    V. M. Mazhul’, S. Zh. Kananovich, and Zh. V. Prokopova, Vestsi NAN Belarusi no. 1, 60 (2001).Google Scholar
  7. 7.
    V. M. Mazhul’ and I. V. Galets, Biofizika 51, 413 (2006).Google Scholar
  8. 8.
    V. M. Mazhul’, Yu. S. Ermolaev, and S. V. Konev, Zh. Prikl. Spektrosk. 32, 903 (1980).Google Scholar
  9. 9.
    V. M. Mazhul’ and D. G. Shcherbin, Proc. SPIE 2980,487 (1997).ADSGoogle Scholar
  10. 10.
    V. M. Mazhul’, E. M. Zaitseva, D. G. Shcherbin, and I. V. Galets, Zh. Prikl. Spektrosk. 70, 346 (2003).Google Scholar
  11. 11.
    J. R. Casey and R. A. F. Reithmeir, Biochemistry 32, 1172 (1993).CrossRefGoogle Scholar
  12. 12.
    M. Maire, P. Champeil, and J. V. Moller, Biochim. Biophys. Acta 1508, 86 (2000).CrossRefGoogle Scholar
  13. 13.
    S. Kopanchuk and A. Rinken, Proc. Estonian Acad. Sci. Chem. 50(4), 229 (2001).Google Scholar
  14. 14.
    S. M. Bhairi, Detergents. A Guide to the Properties and Uses of Detergents in Biological Systems (Calbiochem-Novabiochem, La Jolla, CA, 1997).Google Scholar
  15. 15.
    S. Soulie, J. M. Neumann, C. Berthomieu, et al., Biochemistry 38, 5813 (1999).CrossRefGoogle Scholar
  16. 16.
    G. S. Menzies, K. Howland, M. T. Rae, and T. A. Bramley, Mol. Cell. Endocrinol. 153, 57 (1999).CrossRefGoogle Scholar
  17. 17.
    G. T. Dodge, C. Mitchell, and D. J. Hanahan, Arch. Biochim. Biophys. 100(2), 119 (1963).CrossRefGoogle Scholar
  18. 18.
    M. A. K. Markwell, S. M. Haas, and N. E. Tolbert, Anal. Biochem. 87, 206 (1978).CrossRefGoogle Scholar
  19. 19.
    V. M. Mazhul’, L. S. Ivashkevich, D. G. Shcherbin, et al., Zh. Prikl. Spektrosk. 64, 489 (1997).Google Scholar
  20. 20.
    V. M. Mazhul’ and D. G. Shcherbin, Curr. Topics Biophys. 21(2), 117 (1997).Google Scholar
  21. 21.
    V. M. Mazhul’ and D. G. Shcherbin, Biofizika 43, 456 (1998).Google Scholar
  22. 22.
    J. M. Vanderkooj, in Topics in Fluorecence Spectroscopy, Ed. by J. R. Lacovicz (Plenum Press, New York-London, 1992), vol. 3, pp. 113–136.Google Scholar
  23. 23.
    J. A. Shauere, D. G. Steel, and A. Gafni, Meth. Enzymol. 278, 49 (1997).CrossRefGoogle Scholar
  24. 24.
    P. Cioni and G. B. Strambini, J. Am. Chem. Soc. 120, 11749 (1998).CrossRefGoogle Scholar
  25. 25.
    M. Eilers and A. B. Patel, Biophys. J. 82, 2720 (2002).CrossRefGoogle Scholar
  26. 26.
    M. Olivella, X. Deupi, and C. Govaerts, Biophys. J. 82,3207 (2002).CrossRefGoogle Scholar
  27. 27.
    Yu. F. Krupyanskii, M. G. Mikhailyuk, S. V. Esin, et al., Biofizika 51, 13 (2006).Google Scholar

Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  • V. M. Mazhul’
    • 1
  • I. V. Galets
    • 1
  1. 1.Institute of Biophysics and Cell EngineeringNational Academy of Sciences of BelarusMinskBelarus

Personalised recommendations