Interaction of Bovine Serum Albumin and Hexadecyl Pyridinium Bromide Study by Surfactant Selective Electrode and Spectrophotometry

  • Hossain Naderimanesh
  • Nader Alizadeh
  • Mojtabah Shamsipoor


Surfactant selective electrode and spectrophotometric were used to study the effect of hexadecyl pyridinium bromide (HPB) on the conformation changes of bovine serum albumin (BSA) in aqueous solution. Our previous finding suggested multi-state serum albumin BSA. EMF plots — versus logarithm of HPB concentration revealed also four breaks. The saturated quantities of the HPB binding were 33,93,155,255 mol/mol. The Reynolds and Hill equations were applied to obtain co-operative HPB bindings to BSA. Gibbs free energy was calculated from binding data. Spectrophotometry study suggests hydrophobic interaction of HPB with BSA.


Bovine Serum Albumin Surfactant Concentration Micro Calorimetry Hill Equation Binding Isotherm 
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  1. 1.
    Anson, M.I. (1939) Science 90: 256.PubMedCrossRefGoogle Scholar
  2. 2.
    Pallansch, M.J. and Briggs, D.R. (1954) J. Amer. Chem. Soc. 76: 1396.CrossRefGoogle Scholar
  3. 3.
    Wasylewski, Z. (1979) Acta Biochemica Polonica Vol. 26: No. 3: 195–203.Google Scholar
  4. 4.
    Ancell, H. (1939) Lancet 1: 222–231.Google Scholar
  5. 5.
    Figge, J., Rossing, T.H. and Fencl, V. (1991) J. Lab. Clin. Med. 117: 453–467.PubMedGoogle Scholar
  6. 6.
    Carter, D.C. and Ho, J.X. (1994) Adv.Pro. Chem. 45, 153–203.CrossRefGoogle Scholar
  7. 7.
    Birch, B.J. and Clark, D.E. (1973) Anal. Chem. Acta. 69: 387.CrossRefGoogle Scholar
  8. 8.
    Davidson, C.J. Ph.D. thesis (University of Aberdeen, 1983 ).Google Scholar
  9. 9.
    Painter, D.M., Bloor, D.M., Takisawa, N., Hall, D.G. and Wynjones, E. (1988) J. Chem. Soc. Far. Trans, I, 84: 2087.CrossRefGoogle Scholar
  10. 10.
    Painter, D.M. Ph.D. Thesis (University of Salford, 1988 ).Google Scholar
  11. 11.
    Steinhardt, J., and Reynolds, J.A. (1968) Multiple Equilibiria in Protein, pp. 239–302, Academic press, New York.Google Scholar
  12. 12.
    Reynolds, J.A. Herbert, S., Polet, H. and Steinhardt, (1967) J. Biochemistry 6: 937.CrossRefGoogle Scholar
  13. 13.
    Reynolds, J.A., Gallagher, J.P. and Steinbardt, J. (1970) Biochemisrty 9: 1232.CrossRefGoogle Scholar
  14. 14.
    Takeda, K., Miura, M. and Takagi, T. (1981) J. Colloid Interface Sci. 82: 38.CrossRefGoogle Scholar
  15. 15.
    Wada, A. and Takeda, K. (1990) J. Colloid Interface Sci . 138(1): 277–279.CrossRefGoogle Scholar
  16. 16.
    Wyman, J. (1965) J Mol. Biol. 11: 631–644.PubMedCrossRefGoogle Scholar
  17. 17.
    Hill, A.V. (1910) J. Phsio.Google Scholar
  18. 18.
    Strop, (1987) Chem. Commun. 52 (5): 1362–1374.Google Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Hossain Naderimanesh
    • 1
  • Nader Alizadeh
    • 1
  • Mojtabah Shamsipoor
    • 2
  1. 1.Faculty of ScienceTarbiat Modarres UniversityIran
  2. 2.Department of ChemistryKermanshah UniversityKermanshahIran

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