Skip to main content
SpringerLink
Log in

Native and hydrophobized human IGG: Enthalpies of heat-induced structural changes and adsorption onto silica

  • Published:
Journal of Thermal Analysis and Calorimetry Aims and scope Submit manuscript

Abstract

Differential scanning calorimetry (DSC) and isothermal calorimetric batch technique were used to monitor the heat-induced structural changes and adsorption properties of human immunoglobulin G (IgG), in native and hydrophobized states. The transition temperature (T max) and enthalpy of heat-induced conformational changes (Δcal H) of IgG in solution as well as the enthalpy change accompanying the adsorption of IgG onto hydrophilic silica (Δads H), were shown to depend on the degree of the protein hydrophobicity (number of covalently attached alkyl chains). The adsorption enthalpy for all forms of IgG at all surface concentrations was found to be endothermic, that is the process is entropy driven. Factors affecting the IgG adsorption onto silica are discussed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. A. Kamyshny, Russ. J. Phys. Chem., 55 (1981) 319.

    Google Scholar 

  2. C. A. Haynes and W. Norde, Colloids Surf., B 2 (1994) 517.

    Google Scholar 

  3. J. L. Brash and T. A. Horbett, In Proteins at Interfaces II. Fundamentals and Applications. T. A. Horbett and J. L. Brash Eds ACS Symposium Series, American Chemical Society, Washington DC, 602 (1994) 1.

    Google Scholar 

  4. S. Magdassi and A. Kamyshny, In Surface Activity of Proteins: Chemical and Physicochemical Modifications. S. Magdassi Ed. Marcel Dekker, New York, 1996, Chapter 1, p. 1.

    Google Scholar 

  5. M. A. Esquibel-King, A. C. Dias-Cabral, J. A. Queiroz and N. G. Pinto, J. Chromatogr., 865 (1999) 111.

    Google Scholar 

  6. P. Raje and N. G. Pinto, J. Chromatogr., 796 (1988) 141.

    Google Scholar 

  7. F.-Y. Lin, W.-Y. Chen, R.-C. Ruaan and H.-M. Huang, J. Chromatogr., 872 (2000) 37.

    Google Scholar 

  8. E. Dickinson, Introduction to Food Colloids, Oxford University Press, Oxford 1992.

    Google Scholar 

  9. S. Magdassi and O. Toledano, In Surface Activity of Proteins: Chemical and Physicochemical Modifications. S. Magdassi Ed. Marcel Dekker, New York 1996, Chapter 2, p. 39.

    Google Scholar 

  10. V. R. Sarma, E. W. Silverton, D. R. Davis and W. D. Terry, J. Biol. Chem., 246 (1971) 3753.

    Google Scholar 

  11. I. Pilz, O. Kratky and F. Karush, Eur. J. Biochem., 41 (1974) 91.

    Google Scholar 

  12. J. Deisenhofer, Biochemistry, 20 (1981) 2361.

    Google Scholar 

  13. M. Marquart, J. Deisenhofer, R. Huber and W. Palm, J. Mol. Biol., 141 (1980) 369.

    Google Scholar 

  14. A. Kamyshny and S. Magdassi, Colloids Surf., B 9 (1997) 147.

    Google Scholar 

  15. A. Kamyshny, O. Toledano and S. Magdassi, Colloids Surf., B 13 (1999) 187.

    Google Scholar 

  16. A. Kamyshny, S. Magdassi and P. Relkin, J. Colloid Interface Sci., 212 (1999) 74.

    Google Scholar 

  17. A. W. P. Vermeer, G. E. G. Bremer and W. Norde, Biochim. Biophys. Acta, 1425 (1998) 1.

    Google Scholar 

  18. P. L. Privalov, Adv. Protein Chem., 33 (1979) 167.

    Google Scholar 

  19. J. Lefebvre and P. Relkin, In Surface Activity of Proteins: Chemical and Physicochemical Modifications. S. Magdassi Ed. Marcel Dekker, New York 1996, Chapter 7, p. 181.

    Google Scholar 

  20. V. M. Tishchenko, V. P. Zav'yalov, G. A. Medgyesi, S. A. Potekhin and P. L. Privalov, Eur. J. Biochem., 126 (1982) 517.

    Google Scholar 

  21. J. Buchner, M. Renner, H. Lilie, H.-J. Hinz, R. Jaenicke, T. Kiefhaber and R. Rudolf, Biochemistry, 30 (1991) 6922.

    Google Scholar 

  22. S. P. Maltsev, Z. I. Kravchuk, A. P. Vlasov and G. Lyakhnovich, FEBS Lett., 361 (1995) 173.

    Google Scholar 

  23. W. Norde and J. Lyklema, J. Colloid Interface Sci., 66 (1978) 295.

    Google Scholar 

  24. W. Norde, J. Disp. Sci. Technol., 13 (1992) 363.

    Google Scholar 

  25. F. Galisteo and W. Norde, Colloids Surf., B 4 (1995) 375.

    Google Scholar 

  26. P. Relkin, A. Kamyshny and S. Magdassi, J. Phys. Chem., B 104 (2000) 4980.

    Google Scholar 

  27. A. Kamyshny, S. Lagerge, S. Partyka, P. Relkin and S. Magdassi, Langmuir, 17 (2001) 8242.

    Google Scholar 

  28. E. Harlow and D. Lane, Antibodies. A Laboratory Manual. Cold Spring Harbor Laboratory, New York 1988, p. 283.

    Google Scholar 

  29. Y. Lapidot, S. Rappaport and Y. Wolman, J. Lipid Res., 8 (1967) 142.

    Google Scholar 

  30. A. F. S. Habeeb, Anal. Biochem., 14 (1966) 328.

    Google Scholar 

  31. J. Adler-Nissen, Agric. Food Chem., 27 (1979) 1256.

    Google Scholar 

  32. J. Bradford, Agric. Food Chem., 27 (1979) 248.

    Google Scholar 

  33. G. L. Peterson, Anal. Biochem., 100 (1979) 201.

    Google Scholar 

  34. S. Partyka, M. Lindheimer, S. Zaini, E. Keh and B. Braun, Langmuir, 2 (1986) 101.

    Google Scholar 

  35. E. Harlow and D. Lane, Antibodies. A Laboratory Manual. Cold Spring Harbor Laboratory, New York, 1988, p. 553.

    Google Scholar 

  36. A. K. P. Murphy and E. Freire, Adv. Protein Chem., 222 (1991) 687.

    Google Scholar 

  37. P. Relkin, Int. J. Biol. Macromol., 22 (1997) 59.

    Google Scholar 

  38. W. J. Norde and J. P. Favier, Colloids Surf., 64 (1992) 87.

    Google Scholar 

  39. T. Arai and W. Norde, Colloids Surf., 51 (1990) 1.

    Google Scholar 

  40. P. G. Koutsoukos, W. Norde and J. Lyklema, J. Colloid Interface Sci., 95 (1983) 385.

    Google Scholar 

  41. W. R. Bowen and D. T. Hughes, J. Colloid Interface Sci., 158 (1993) 395.

    Google Scholar 

  42. D. S. Gill, D. J. Roush, K. A. Shick and R. C. Willson, J. Chromatogr., 715 (1995) 81.

    Google Scholar 

  43. C. A. Haynes and W. Norde, J. Colloid Interface Sci., 169 (1995) 313.

    Google Scholar 

  44. B. L. Steadman, K. C. Thomson, C. R. Middaugh, K. Matsuno, S. Vrona, E. Q. Lawson and R. V. Lewis, Biotechnol. Bioeng., 40 (1992) 8.

    Google Scholar 

  45. H. Larsericsdotter, S. Oscarsson and J. J. Buijs, J. Colloid Interface Sci., 237 (2001) 98.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Casali Institute of Applied Chemistry, The Hebrew University of Jerusalem, 91904, Israel

    A. Kamyshny & S. Magdassi

  2. Laboratoire de Biophysique des Matériaux Alimentaires, Ecole Nationale Supérieure des Industries Alimentaires, 1, Avenue des Olympiades, F-91744, Massy, France

    P. Relkin

  3. LAMMI, ESA 5072, Université de Montpellier II Case 015, 2 Place E. Bataillon, 34095, Montpellier Cedex 05, France

    S. Lagerge & S. Partyka

Authors
  1. A. Kamyshny
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. P. Relkin
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. S. Lagerge
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. S. Partyka
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. S. Magdassi
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to A. Kamyshny.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Kamyshny, A., Relkin, P., Lagerge, S. et al. Native and hydrophobized human IGG: Enthalpies of heat-induced structural changes and adsorption onto silica. Journal of Thermal Analysis and Calorimetry 71, 263–272 (2003). https://doi.org/10.1023/A:1022247107779

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1022247107779

Search

Navigation