Affinity determinations of purified IgE and IgG antibodies against the major pollen allergens Phl p 5a and Bet v 1a: discrepancy between IgE and IgG binding strength.

@article{Hantusch2005AffinityDO,
  title={Affinity determinations of purified IgE and IgG antibodies against the major pollen allergens Phl p 5a and Bet v 1a: discrepancy between IgE and IgG binding strength.},
  author={Brigitte Hantusch and Isabella Schoell and Christian Harwanegg and Sigurd Krieger and W. Becker and Susanne Spitzauer and G Boltz-nitulescu and Erika Jensen-Jarolim},
  journal={Immunology letters},
  year={2005},
  volume={97 1},
  pages={
          81-9
        }
}
  • Brigitte Hantusch, Isabella Schoell, +5 authors Erika Jensen-Jarolim
  • Published in Immunology letters 2005
  • Biology, Medicine
  • Allergen-specific IgE and IgG antibodies coexist in allergic individuals, but only IgE has anaphylactogenic capacity. This study aimed to determine the association, dissociation and equilibrium constants for the interaction of allergen-specific IgE and IgG with the major grass and birch pollen allergens Phl p 5a and Bet v 1a. We isolated specific IgE and IgG antibodies from pollen allergic patients' sera by a two-step affinity chromatography protocol and controlled the high purity in a… CONTINUE READING

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