Advertisement

Enzymes and Nucleic Acids Solubilized in Hydrocarbon Solvents with the Help of Reverse Micelles

  • P. L. Luisi
  • P. Meier
  • V. E. Imre
  • A. Pande
Chapter
Part of the Forschung Soziologie book series

Abstract

Various aspects of the reverse micellar systems have been discussed in these Proceedings. In general, they can be divided into two main classes: i) structural and thermodynamic studies, and ii) study of reactivity and function. Our contribution belongs to the latter class. In particular, we like to view reverse micelles as microreactors, whose dimensions and physical properties can be altered by changing the water content of the macroscopic system. Of interest to us are questions related to the peculiarities of these microreactors, namely, a) whether and to what extent they confer novel structural and reactivity properties to guest molecules, and b) whether these microreactors can be useful either for biotechnology or as biological models. In a previous review1 we have discussed various structural and reactivity properties of enzymes solubilized in AOT reverse micelles (AOT = bis(2-ethylhexyl) sodium sulfosuccinate). In this article we would like to review our recent work in the area, emphasizing in particular the characterization and purity of AOT reverse micelles.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    P.L. Luisi and R. Wolf, in “Solution Behavior of Surfactants, Vol. 2, K.L. Mittal and E.J. Fendler, Eds., Plenum Publishing Corp., New York (1982).Google Scholar
  2. 2.
    P.D.I. Fletcher, N.F. Perrins, B.H. Robinson and C. Toprakcioglu, in these Proceedings.Google Scholar
  3. 3.
    C.A. Martin and L.J. Magid,. J. Phys. Chem., 85: 3938 (1981).CrossRefGoogle Scholar
  4. 4.
    M. Wong, J.K. Thomas and M. Grätzel, J. Am. Chem. Soc., 98: 2391 (1976).CrossRefGoogle Scholar
  5. 5.
    F.J. Bonner, R. Wold and P.L. Luisi, J. Solid-Phase Biochem., 5: 255 (1980).CrossRefGoogle Scholar
  6. 6.
    R.E. Smith and P.L. Luisi, Helv. Chimica Acta, 63: 3202 (1980).CrossRefGoogle Scholar
  7. 7.
    S. Barbaric and P.L. Luisi, J. Am. Chem. Soc., 103: 4239 (1981).CrossRefGoogle Scholar
  8. 8.
    C. Grandi, R.E. Smith and P.L. Luisi, J. Biol. Chem. 256: 837 (1981).Google Scholar
  9. 9.
    P. Douzou, Adv. in Enzymology, 51: 1 (1980).Google Scholar
  10. 10.
    F. Nome, S.A. Chang and J.H. Fendler, J. Colloid Interface Sci., 56: 146 (1976).CrossRefGoogle Scholar
  11. 11.
    J.H. Fendler, “Membrane Mimetic Chemistry”, Chapter 3, Wiley-Interscience, New York (1982).Google Scholar
  12. 12.
    O.A. El Seoud, in these Proceedings.Google Scholar
  13. 13.
    C. Balny and P. Douzou, Biochemie, 61: 445 (1979).Google Scholar
  14. 14.
    H.-F. Eicke and P. Kvita, in these Proceedings.Google Scholar
  15. 15.
    L.M. Gierasch and K.F. Thompson, in these Proceedings.Google Scholar
  16. 16.
    L. Goldstein, Y. Levin and E. Katchalski, Biochemistry, 3: 1913 (1964).CrossRefGoogle Scholar
  17. 17.
    V.E. Imre and P.L. Luisi, Biochem. Biophys. Res. Commun., 107: 538 (1982).CrossRefGoogle Scholar
  18. 18.
    J. Brahms, A.M. Michelson and K.E. Van Holde, J. Mol. Biol., 15: 467 (1966).CrossRefGoogle Scholar
  19. 19.
    L.S. Lerman, in “Physico Chemical Properties of Nucleic Acids”, J. Duchesne, Editor, Vol. 3, 59–76, Academic Press, London, New York (1973).Google Scholar
  20. 20.
    B.H. Robinson and P.D.I. Fletcher, personal communication.Google Scholar
  21. 21.
    P. Meier and P.L. Luisi, J. Solid-Phase Biochem., 5: 269 (1980).CrossRefGoogle Scholar
  22. 22.
    K. Martinek, A.V. Levashov, N.L. Klyachko, V.I. Pantin and I.V. Berezin, Biochem. Biophys. Acta, 657: 277 (1981).Google Scholar
  23. 23.
    F.M. Menger and K. Yamada, J. Am. Chem. Soc., 101: 6731 (1979).CrossRefGoogle Scholar
  24. 24.
    A. Pande, H. Gablinger and P.L. Luisi,unpublished results.Google Scholar
  25. 25.
    K. Martinek, A.V. Levashov, Y.L. Khmelnitsky, N.L. Klyachko and I.V. Berezin, Science, 218: 889 (1982).CrossRefGoogle Scholar
  26. 26.
    D. Findlay, A.P. Mathias and B.R. Rabin, Biochem. J., 85: 139 (1962).Google Scholar
  27. 27.
    A. Fersht, “Enzyme Structure and Mechanism”, p. 90, W.H. Freeman and Company, California (1977).Google Scholar
  28. 28.
    P.D.I. Fletcher, A.M. Howe, B.H. Robinson and D.C. Steytler, in these Proceedings.Google Scholar
  29. 29.
    R. Hillhorst, C. Laane and C. Veeger, manuscript in preparation.Google Scholar
  30. 30.
    P. Meier, Dissertation (ETH Nr. 7222) (1983).Google Scholar
  31. 31.
    K. Simons, H. Garoff and A. Helenius, Sci. Am., 246 (2): 46 (1982).CrossRefGoogle Scholar
  32. 32.
    R.W. Horne, Sci. Am., 280 (1): 48 (1963).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1984

Authors and Affiliations

  • P. L. Luisi
    • 1
  • P. Meier
    • 1
  • V. E. Imre
    • 1
  • A. Pande
    • 1
  1. 1.Technisch-Chemisches LaboratoriumETH-ZentrumZurichSwitzerland

Personalised recommendations