Egg proteins represent one of the most important sources evoking food allergic reactions. In order to improve allergy diagnosis, purified and well-characterized proteins are needed. Although the egg white allergens Gal d 1, 2, 3 and 4 (ovomucoid, ovalbumin, ovotransferrin, and lysozyme) are commercially available, these preparations contain impurities, which affect exact in vitro diagnosis. The aim of the present study was to set up further purification protocols and to extend the characterization of the physicochemical and immunological properties of the final batches. The egg white allergens Gal d 1–4 were purified from commercial preparations, whereas Gal d 5 (a-livetin) was purified from egg yolk. The final batches of Gal d 1–5 consisted of a range of isoforms with defined tertiary structure. In addition, the IgE binding capacity of the purified egg allergens was tested using allergic patients’ sera. The allergen batches will be further used to set up allergen specific diagnostic assays and to screen a larger collection of patients’ sera.

The panel of egg allergens, Gal d 1 - Gal d 5: Their improved purification and characterization / B. Jacobsen; K. Hoffmann-Sommergruber; T. Thordahl Have; N. Foss; P. Briza; C. Oberhuber; C. Radauer; S. Alessandri; A. C. Knulst; M. Fernandez-Rivas; V. Barkholt. - In: MOLECULAR NUTRITION & FOOD RESEARCH. - ISSN 1613-4125. - STAMPA. - Volume 52 Issue S2:(2008), pp. 176-185. [10.1002/mnfr.200700414]

The panel of egg allergens, Gal d 1 - Gal d 5: Their improved purification and characterization

ALESSANDRI, STEFANO;
2008

Abstract

Egg proteins represent one of the most important sources evoking food allergic reactions. In order to improve allergy diagnosis, purified and well-characterized proteins are needed. Although the egg white allergens Gal d 1, 2, 3 and 4 (ovomucoid, ovalbumin, ovotransferrin, and lysozyme) are commercially available, these preparations contain impurities, which affect exact in vitro diagnosis. The aim of the present study was to set up further purification protocols and to extend the characterization of the physicochemical and immunological properties of the final batches. The egg white allergens Gal d 1–4 were purified from commercial preparations, whereas Gal d 5 (a-livetin) was purified from egg yolk. The final batches of Gal d 1–5 consisted of a range of isoforms with defined tertiary structure. In addition, the IgE binding capacity of the purified egg allergens was tested using allergic patients’ sera. The allergen batches will be further used to set up allergen specific diagnostic assays and to screen a larger collection of patients’ sera.
2008
Volume 52 Issue S2
176
185
B. Jacobsen; K. Hoffmann-Sommergruber; T. Thordahl Have; N. Foss; P. Briza; C. Oberhuber; C. Radauer; S. Alessandri; A. C. Knulst; M. Fernandez-Rivas; V. Barkholt
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/349044
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