Chemistry of Natural Compounds

, Volume 27, Issue 6, pp 731–735 | Cite as

Immunoaffinity fractionation of neutralizing polyclonal antibodies to nerve growth factors

  • D. Kh. Khamidov
  • A. V. Lim
  • R. S. Salikhov
  • M. Sh. Akramov


A method of fractionation according to affinity and specificity of polyclonal antibodies to murine and ovine nerve growth factors (NGFs) has been developed. The antibody preparations obtained neutralize the biological activity of β-NGF at a molar ratio of about 1 and recognize the species-specific and conservative epitopes of these NGFs, being valuable probes for two-site immunoanalyses.


Nerve Growth Factor Neutralize Activity Glucose Isomerase Biological Unit Uzbek Academy 


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Literature cited

  1. 1.
    R. Levi-Montalcini, Science,237, 1154–1162 (1987).CrossRefPubMedGoogle Scholar
  2. 2.
    T. Ebendal, Progr. Growth Factor Res.,1, 143–159 (1989).CrossRefGoogle Scholar
  3. 3.
    J. R. Perez-Polo, K. Werrbach-Perez, D. Marchetti, B. Morgan, G. Tagliatela, M. T. Ramacci, and L. Angelucci, Int. J. Clin. Pharm. Res.,10, No. 1–2, 15–26 (1990).Google Scholar
  4. 4.
    V. N. Kalynov, Nerve Tissue Growth Factor [in Russian], Nauka Tekh., Minsk (1984).Google Scholar
  5. 5.
    V. Bocchini and P. U. Angeletti, Proc. Natl. Acad. Sci. USA,64, 787–794 (1969).CrossRefPubMedGoogle Scholar
  6. 6.
    R. Hogue-Angeletti, Proc. Natl. Acad. Sci. USA,65, 668–674 (1970).CrossRefGoogle Scholar
  7. 7.
    J. Siigur, U. Arumae, T. Neuman, M. Samel, R. Siigur, and M. Saarma, Comp. Biochem. Physiol.,83B, No. 3, 621–625 (1986).Google Scholar
  8. 8.
    D. Kh. Khamidov, L. Ya. Yukel'son, R. S. Salikhov, and M. G. Khafizova, Biokhimiya,54, No. 6, 987–991 (1989).Google Scholar
  9. 9.
    G. P. Harper, R. W. Glanville, and H. Thoenen, J. Biol. Chem.,257, 8541–8548 (1982).PubMedGoogle Scholar
  10. 10.
    S. N. Olenev, Arkh. Anat. Gistol. Émbriol., No. 9, 19–29 (1969).Google Scholar
  11. 11.
    K. Suda, Y. A. Barde, and H. Thoenen, Proc. Natl. Acad. Sci. USA,75, 4042–4046 (1978).CrossRefPubMedGoogle Scholar
  12. 12.
    K. Stoeckel, C. Gagnon, G. Guroff, and H. Thoenen, J. Neurochem.,26, 1207–1211 (1976).CrossRefPubMedGoogle Scholar
  13. 13.
    A. Ullrich, A. Gray, C. Berman, and T. J. Dull, Nature (London),303, 821–825 (1983).CrossRefPubMedGoogle Scholar
  14. 14.
    A. Cattaneo, B. Rapposelli, and P. Calissano, J. Neurochem.,50, 1003–1010 (1988).CrossRefPubMedGoogle Scholar
  15. 15.
    O. Ouchteroni, Progr. Allergy,4, 30–154 (1954).Google Scholar
  16. 16.
    O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem.,193, 265–275 (1951).PubMedGoogle Scholar

Copyright information

© Plenum Publishing Corporation 1992

Authors and Affiliations

  • D. Kh. Khamidov
  • A. V. Lim
  • R. S. Salikhov
  • M. Sh. Akramov

There are no affiliations available

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