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Recognition of an extensive range of IgE‐reactive proteins in cod extract
Author(s) -
Dory D.,
Chopin C.,
AimoneGastin I.,
Gueant J. L.,
Guerin L.,
SainteLaudy J.,
MoneretVautrin D. A.,
Fleurence J.
Publication year - 1998
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/j.1398-9995.1998.tb03772.x
Subject(s) - western blot , immunoglobulin e , allergen , chemistry , rigor mortis , blot , allergy , biochemistry , microbiology and biotechnology , antibody , chromatography , biology , immunology , gene
Allergy to fish is one of the most common food allergies. Gad c 1 is the only fish allergen which has been purified and characterized. Other allergens have been detected by Western blot in cod extracts. We have now improved the Western‐blot procedure in order to characterize fish IgE‐reactive proteins from extracts prepared under different conditions: pre‐rigor mortis and postrigor mortis. EDTA addition or not. and DEAE ion‐exchange chromatography. Several IgE‐reactive protein bands have been identified over a wide molecular‐weight range. In particular, the 104‐ and 130‐kDa IgEreactive protein bands were detected. These new bands may correspond to aggregates, as EDTA increased the relative amount of the 60‐, 67‐, 104‐, and 130‐kDa IgE‐reactive protein bands in Western blot. All these bands were also detected by an antiparvalbumin monoclonal antibody, specific to the first calcium‐binding site. The longer period of storage increased the relative amounts of the 41‐, 80‐, 104‐. and 130‐kDa IgE‐reactive protein bands. The 18‐kDa band was detected only in fish stored for several days. In conclusion, we have described IgE‐reactive protein bands over a wide molecular‐weight range (12–130 kDa) in Western blot of cod extract, and shown that EDTA and storage conditions may influence the relative distribution of IgE‐reactive protein bands.