Quirce et al. (2001) [1268] found that cooking reduces but does not eliminate allergenicity (a 10-fold higher concentration was needed for 50% inhibition in IgE ELISA-inhibition assays).
Nature of main cross-reacting proteins:
Quirce et al. (2001) [1268] reported some cross-reactivity with Gal d 3, ovotranferrin, which at high concentration partially inhibited IgE binding to chicken serum albumin in ELISA-inhibition assays. However, it hard to purify alpha-livetin free of ovotransferrin.
Allergen properties & biological function:
Serum albumins are a major component of blood plasma and bind both ions, Ca(2+), Na(+), K(+), and hydrophobic molecules, such as fatty acids, hormones, and drugs. Consequently it is also found in meat. Serum albumins are present at a lower concentration in egg.
Allergen purification:
Commercial preparations of serum albumin (alpha-livetin) often use Cohn fractionation with cold ethanol (fraction 5). The commercial material or that from Cohn fractionation is generally purified further by chromatography. Predki et al. (1992) [1405] treated fraction V powder with charcoal and fractionated twice on Sephadex G-100 in 50 mM Tris/HCl, pH 7.4.
Other biochemical information:
References (4)
de Blay F, Hoyet C, Candolfi E, Thierry R, Pauli G.
Identification of alpha livetin as a cross reacting allergen in a bird-egg syndrome.
Allergy Proc. 15(2):77-78. 1994
PUBMED ID:
8034193
Predki PF, Harford C, Brar P, Sarkar B.
Further characterization of the N-terminal copper(II)- and nickel(II)-binding motif of proteins. Studies of metal binding to chicken serum albumin and the native sequence peptide.
Biochem J. 287 ( Pt 1):211-215.
1992
PUBMED ID:
1417775
Quirce S, Maranon F, Umpierrez A, de las Heras M, Fernandez-Caldas E, Sastre J.
Chicken serum albumin (Gal d 5) is a partially heat-labile inhalant and food allergen implicated in the bird-egg syndrome.
Allergy 56(8):754-762.
2001
PUBMED ID:
11488669
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