IgE-binding and cross-reactivity of a new 41 kDa allergen of codfish

S. Das Dores, C. Chopin, A. Romano, A. V. Galland-Irmouli, D. Quaratino, C. Pascual, J. Fleurence, J. L. Guéant

Research output: Contribution to journalArticlepeer-review


Background: A 41-kDa IgE-reactive protein (p41) was purified from raw cod extract. This protein is homologous to an aldehyde phosphate dehydrogenase (APDH). The present study aims to evaluate the IgE-binding and the cross-reactivity of this protein in 13 patients allergic to codfish. Methods: IgE binding of sera from 13 patients allergic to codfish was tested by Sepharose RIA and by Western blot. Results: Among the 13 patients, only 4 had specific IgE to APDH detected by APDH-Sepharose RIA. The two patients who had the highest level of specific IgE to human APDH also had a class 5-6 CAP-RAST IgE level to codfish, but two other patients with a class 5 had a negative APDH-Sepharose IgE-RIA. Relative content of APDH was higher in extracts of commercial nonfrozen fish, compared to pre rigor mortis, post rigor mortis and frozen commercial codfish. A high homology of codfish APDH was found with the corresponding human enzyme. A significant inhibition of APDH-Sepharose by human and, to a lesser extent, by rabbit APDH was observed. Western blot of APDH codfish extract showed two bands at 41 and 36 kDa, respectively. Conclusions: We have characterized a new allergen from codfish, which had a high level of homology in different species. The p41 relative content of extracts from nonfrozen codfish was higher than in the other samples assessed.

Original languageEnglish
Pages (from-to)84-87
Number of pages4
JournalAllergy: European Journal of Allergy and Clinical Immunology, Supplement
Issue number72
Publication statusPublished - Sep 2002


  • Codfish
  • Dehydrogenase
  • Food allergy
  • IgE

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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