IgG Subclass Distribution in Juvenile Human Tonsil: IgG3 and IgG4 Results of Specific Antibody Production Using Synthetic Peptides

  • W. J. A. Boersma
  • C. Deen
  • N. D. Zegers
  • J. Radl
  • J. J. Haaijman
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 237)


A decapeptide with a sequence corresponding to a part of the hinge region of human IgG3 was used to prepare a mouse monoclonal antibody (Mab 330-2.2). The Mab recognized IgG3 in ELISA only when the IgG3 was denatured by mild heat. Mab specificity in immunohistochemistry was calibrated with a number of reference Mabs obtained through a WHO/IUIS collaborative study. Finally, Mab 330-2.2 was used in conjunction with a set of other isotype specific Mabs to study the (sub) class distribution of cytoplasmic Ig containing cells in palatine tonsil. IgG3 within the IgG class was strongly over-represented in our tonsil material if compared to the representation of IgG3 in serum.


Hinge Region Palatine Tonsil Immunology Today Native IgG3 Repeated Amino Acid Sequence 
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  1. 1.
    Pumphrey R., Immunology Today, 7: 14 (1986)Google Scholar
  2. 2.
    Kabat E.A., Wu T.T., Bilofsky H., Reid-Miller M., Perry H., Sequences of proteins of immunological interest. U.S. Department of Health and Human Services (1983)Google Scholar
  3. 3.
    Jefferis R. et al., Immunology Letters 10: 223 (1985)PubMedCrossRefGoogle Scholar
  4. 4.
    Westhof E., Altschuh D., Moras D., Bloomer A.C., Mondragon A., Klug A., van Regenmortel M.H.V., Nature 311: 123 (1984)PubMedCrossRefGoogle Scholar
  5. 5.
    Tainer J.A., Getzoff E.D., Alexander H., Houghten R.A., Olson A.J., Lerner R.A. Hendrickson W.A., Nature 312: 127 (1984)PubMedCrossRefGoogle Scholar
  6. 6.
    Haaijman J.J., Coolen J., Deen C, Kröse C.J.M., Zijlstra J.J., Radl J., In: Pal, S.B. (ed) Reviews on immunoassay technology. The MacMillan Press Ltd. London, U.K., 1987, in pressGoogle Scholar
  7. 7.
    Haaijman J.J. Coolen J., Kröse C.J.M., Pronk G.J., Ming Z.F., Histochemistry 84: 363 (1986)PubMedCrossRefGoogle Scholar
  8. 8.
    Haaijman J.J., Deen C, Kröse C.J.M., Zijlstra J.J., Coolen J., Radl J., Immunology Today 5: 56 (1984)CrossRefGoogle Scholar
  9. 9.
    Hijmans W., Schuit H.R.E., Hulsing-Hesselink E., Ann. N.Y. Acad. Sci. 177: 290, (1971)PubMedCrossRefGoogle Scholar
  10. 10.
    Brandtzaeg P., Surjan L., Berdal P., Clin. Exp. Immunol. 31: 367 (1978)PubMedGoogle Scholar
  11. 11.
    Surjan L., Brandtzaeg P., Berdal P., Clin. Exp. Immunol. 31: 382 (1978)PubMedGoogle Scholar
  12. 12.
    Kett K., Brandtzaeg P., Radl J., Haaijman J.J., J. Immunol. 136: 3681 (1986)Google Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • W. J. A. Boersma
    • 1
  • C. Deen
    • 1
  • N. D. Zegers
    • 1
  • J. Radl
    • 2
  • J. J. Haaijman
    • 1
  1. 1.Medical Biological Lab. TNORijswijkThe Netherlands
  2. 2.Institute for Experimental Gerontology TNORijswijkThe Netherlands

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