Immunochemical Properties of Native and Heat Denatured Ovalbumin

Breton, C.; Thanh, Luu Phan; Paraf, A

doi:10.1111/j.1365-2621.1988.tb10214.x

Cited by 28 publications

(19 citation statements)

References 14 publications

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“…The allergenicity of OA was changed by heating or pepsin treatment. The primary structure of OA is not changed by heating [18] or pepsin treatment [10] [20]. Breton et al described that native OA was found as a single band of 45 kd, and heat-denatured OA was also found as a single band of 45 kd as judged by SDS-PAGE analysis.…”

Section: Discussionmentioning

confidence: 99%

Proliferative responses towards native, heat-denatured and pepsin-treated ovalbumin by peripheral blood mononuclear cells from patients with hen's egg-sensitive atopic dermatitis

et al. 1994

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In order to clarify the mechanism of food-antigen recognition, the proliferative responses of peripheral blood mononuclear cells (PBMCs) to native, heat-denatured or pepsin-treated ovalbumin (OA) were investigated in 16 hen's egg-sensitive patients with atopic dermatitis (AD). Seven of them had hypersensitivity to boiled hen's egg and others had not. The responses of PBMCs to heat-denatured OA were lower than those to native OA in the patients without hypersensitivity to boiled hen's egg. However, there were no differences of the responses of PBMCs between heat-denatured OA and native OA in the patients with hypersensitivity to boiled hen's egg. Moreover, the reduction of the responses of PBMCs to pepsin-treated OA was recognized in six out of seven patients. The primary structure of OA did not change by heating or pepsin treatment according to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). These results suggested that the secondary structure of OA changed in connection with the reduction of the responses of PBMCs to denatured OA. In addition, we demonstrated the suppressive effect of anti-HLA-DR and anti-HLA-DQ monoclonal antibodies on the proliferative response of PBMCs to OA. The results suggested that the proliferative responses of PBMCs to OA were restricted by HLA-DR or HLA-DQ in hen's egg-sensitive patients with AD.

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Section: Discussionmentioning

confidence: 99%

Proliferative responses towards native, heat-denatured and pepsin-treated ovalbumin by peripheral blood mononuclear cells from patients with hen's egg-sensitive atopic dermatitis

et al. 1994

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“…Commercial products are available for a few selected applications only, e.g. ovalbumin from eggs [19]. Before detection with the specific antibodies, immunoanalytical determinations require appropriate sample preparation.…”

Section: Immunoanalytical Techniquesmentioning

confidence: 99%

Immunoanalytical detection of allergenic proteins in food

Krska¹,

Welzig²,

Baumgartner³

2004

Analytical and Bioanalytical Chemistry

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“…Similar results have been reported in several other studies. Breton et al (1988) demonstrated that, when determined by ciELISA using anti-OA antibody, the detection limit of heat-denatured OA was 0.01 µg/mL although that of native OA was 0.1 µg/mL. They explained these results as follows during heat denaturation, OA can form new epitopes that are available to anti-OA antibody with the same specificity as those detected on the native structure of the antigen.…”

Section: Resultsmentioning

confidence: 84%

“…This change can affect antibody recognition toward antigen proteins (Breton et al, 1988;Samarajeewa et al, 1991). Therefore, we attempted to develop a reliable ELISA system for the quantification of egg proteins, regardless of heat treatment.…”

Section: Resultsmentioning

confidence: 99%

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Enzyme-linked Immunosorbent Assay for the Detection of Hen's Egg Proteins in Processed Foods

Shon¹,

Kim²,

Kim³

et al. 2010

Korean Journal for Food Science of Animal Resources

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The Hen's egg is widely used in many processed foods as an ingredient and is one of the most prevalent food allergens in children. To detect egg proteins in processed foods, we developed a competitive indirect enzyme-linked immunosorbent assay (ciELISA) using an anti-ovomucoid (OM) antibody, which was produced by immunization of rabbits with OM, the most heat-stable component of the egg proteins. The detection limit of this quantitative assay system was 30 ng/mL. Crossreactivity of the anti-OM antibody toward OM, ovalbumin, skim milk, casein, whey protein isolate, and isolated soy protein was 100, 0.4, 0.2, 0.04, 0, and 0%, respectively. In the spike test of egg white powder in milk replacer, commercial sausage, and in-house sausage, the assay recoveries (mean±SD) were 129±13.7%, 73.9±12.5%, and 65.5±13.6%, respectively. When egg white in a commercial crab meat analog and sausage was determined by ciELISA, the assay recovery was found to be 108% and 127%, respectively. The combined results of this study indicate that this novel ciELISA for OM detection could be applied for the quantification of hen's egg proteins in processed foods.

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Immunochemical Properties of Native and Heat Denatured Ovalbumin

Cited by 28 publications

References 14 publications

Proliferative responses towards native, heat-denatured and pepsin-treated ovalbumin by peripheral blood mononuclear cells from patients with hen's egg-sensitive atopic dermatitis

Proliferative responses towards native, heat-denatured and pepsin-treated ovalbumin by peripheral blood mononuclear cells from patients with hen's egg-sensitive atopic dermatitis

Immunoanalytical detection of allergenic proteins in food

Enzyme-linked Immunosorbent Assay for the Detection of Hen's Egg Proteins in Processed Foods

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