scholarly journals Allergy to egg whites: diagnosis, symptoms (clinical features), prognosis

2018 ◽  
Vol 15 (2) ◽  
pp. 5-10
Author(s):  
A V Kudryavtseva ◽  
Y A Boguslavskaya
Keyword(s):  
Food Allergy ◽  
Skin Testing ◽  
Egg Yolk ◽  
Molecular Diagnostic ◽  
Prick Test ◽  
Heat Treated ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Measles Vaccination ◽  
Protein Components

Allergic reactions to hen’s egg are rather a common problem, especially in infants. Hen’s eggs contain a few protein components which may serve as food allergens. They are 4 egg-white proteins: ovomucoid (Gal d 1, 11%), ovalbumin (Gal d 2, 54%), ovotransferrin (Gal d 3, 12%), lysozyme (Gal d 4, 3,4%) and one egg-yolk protein - alpha-livetin (Gal d 5). Ovomucoid (OVM) is the dominant allergen in hen’s egg. The allergenicity of egg whites depends mostly on their resistance to heat and digestive enzymes. A skin prick test size of 5 mm in children younger than 2 years old and 7 mm in children older than 2 years had a positive predicative value (PPV) of 100%. However, patient questioning and skin testing cannot be the only proof of food allergy. There exists a positive correlation between the growing levels of eggs-pecific IgE and the probability of allergic symptoms occurrence. Testing for sensitization to different hen’s egg proteins (molecular diagnostic) may assist in marking off allergy reaction to raw eggs from that one to heat-treated eggs. Questionable cases call for carrying out challenge tests which are not certified in Russia. The recent studies have demonstrated the safety of measles vaccination in children with proven eggwhite allergy. Currently, oral, sublingual and epicutaneous immunotherapy for food allergy to egg-whites has been extensively investigated in clinical trials.

scholarly journals Extractability, Stability, and Allergenicity of Egg White Proteins in Differently Heat-Processed Foods

2007 ◽  
Vol 90 (2) ◽  
pp. 427-436 ◽  
Author(s):  
Christiane K Fste ◽  
Kjersti E Lvberg ◽  
Helene Lindvik ◽  
Eliann Egaas
Keyword(s):  
Egg White ◽  
Food Samples ◽  
Processed Foods ◽  
Heat Treated ◽  
Extraction Buffer ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Study Results ◽  
The Stability ◽  
Protein Extractability

Abstract Hen's egg white protein is a major cause of food allergy, and a considerable number of countries have introduced labeling directions for processed food products. To control compliance with these regulations, analytical assays for the detection of egg in manufactured foods have been developed. In this study, we have tested the performance of 3 commercially available kits for quantitative egg analysis using 6 model heat-processed foods. The 3 assays worked well under standard conditions with soluble egg white proteins, but only the kit using a denaturing-reducing extraction buffer detected egg in complex heat-treated food matrixes. The differently extracted food samples were further used to evaluate the stability and allergenicity of the egg white allergens ovalbumin, ovomucoid, ovotransferrin, and lysozyme with polyclonal anti-egg antibodies and sera of 6 patients with egg allergy. It could be shown that differences in egg protein extractability have a significant impact on the interpretation of study results.

ULTRACENTRIFUGAL ANALYSIS OF YOLK PROTEINS IN RAINBOW TROUT EGG AND THEIR CHANGES DURING DEVELOPMENT

1965 ◽  
Vol 43 (3) ◽  
pp. 373-379 ◽  
Author(s):  
Kazuo Ando
Keyword(s):  
Molecular Weight ◽  
Rainbow Trout ◽  
Phosphorus Content ◽  
Sedimentation Coefficient ◽  
Egg Yolk ◽  
Yolk Proteins ◽  
Hen’S Egg ◽  
Synchronous Development ◽  
Protein Components ◽  
Ultracentrifugal Analysis

Yolk proteins in Salmo irideus (rainbow trout) eggs were studied by means of ultracentrifugal analysis, and the following facts were clarified. Unfertilized eggs contain two protein components, designated as component I (90% in relative content) and component II (10%). The sedimentation constant for component I is 9.4 S and its molecular weight is approximately 240,000 ~ 260,000. The phosphorus and lipid contents of this major component are similar to those of a lipovitellin in hen's egg yolk, but the molecular weight is considerably smaller than that of the hen's lipovitellin. Component I is split by alkali into two subunits. The sedimentation coefficient for the subunits is 4.9 S and the molecular weight is approximately 120,000. The sedimentation coefficient for component II is 3.1 S, and the phosphorus content is higher than that of component I but is lower than that of hen's phosvitin. A new component of 11.2 S appears at the beginning of the eyed stage, and is inferred to be a protein in the blood formed at this stage. The relative changes of these three components during the synchronous development of embryo from fertilization to the swim-up fry stage were followed.

6,8-Dihydroxypurine in the Hen’s Egg Yolk

1973 ◽  
Vol 28 (7-8) ◽  
pp. 482-483
Author(s):  
S. De Boeck ◽  
T. Rymen ◽  
J. Stockx
Keyword(s):  
Egg Yolk ◽  
Hen’S Egg

Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

1968 ◽  
Vol 46 (8) ◽  
pp. 983-988 ◽  
Author(s):  
J. Z. Augustyniak ◽  
W. G. Martin
Keyword(s):  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Egg Yolk ◽  
Low Density ◽  
Amide Nitrogen ◽  
Acetylneuraminic Acid ◽  
Hen’S Egg ◽  
Terminal Amino ◽  
Protein Moiety

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 103. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 103. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.

Peptic digestibility of raw and heat-coagulated hen's egg white proteins at acidic pH range

2004 ◽  
Vol 55 (8) ◽  
pp. 635-640 ◽  
Author(s):  
Kenji Yoshino ◽  
Kentaro Sakai ◽  
Yoko Mizuha ◽  
Ayako Shimizuike ◽  
Shigeru Yamamoto
Keyword(s):  
Egg White ◽  
Acidic Ph ◽  
Egg White Proteins ◽  
Hen’S Egg ◽  
Ph Range
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