TY - JOUR
T1 - The panel of egg allergens, Gal d 1-Gal d 5: Their improved purification and characterization
AU - Jacobsen, B.
AU - Hoffmann-Sommergruber, K.
AU - Have, T. T.
AU - Foss, N.
AU - Briza, P.
AU - Oberhuber, C.
AU - Radauer, C.
AU - Alessandri, S.
AU - Knulst, A.C.
AU - Fernandez-Rivas, M.
AU - Barkholt, Vibeke
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
KW - Egg
KW - Allergens
KW - Purification
KW - NMR
KW - pI
U2 - 10.1002/mnfr.200700414
DO - 10.1002/mnfr.200700414
M3 - Journal article
C2 - 18763254
SN - 1613-4125
VL - 52
SP - S176-S185
JO - Molecular Nutrition and Food Research
JF - Molecular Nutrition and Food Research
ER -