Studies on the Atopic Allergen in Hen's Egg

Bleumink, E.; Young, E.

doi:10.1159/000230396

Cited by 35 publications

(2 citation statements)

References 6 publications

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“…Ovomucoid (OM), a glycoprotein in egg white, is a major allergen of eggs. 2 ) The primary structure of OM is known 3 ); it consists of three homologous domains (domain I (DI), domain II (DII), and domain III (DIll)) that have heterogenous sugar chains. 4 ) To study the antigenic sites of OM, we had prepared, purified, and characterized two monoclonal antibodies (mAb 23E5 and mAb 32A8) against OM.…”

Section: Comparison Of Four Distinct Idiotypes Of Monoclonal Antibodimentioning

confidence: 99%

Comparison of Four Distinct Idiotypes of Monoclonal Antibodies against Hen’s Egg Ovomucoid

Enomoto

Aoki

Kurisaki

et al. 1987

Agricultural and Biological Chemistry

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Two monoclonal antibodies (mAb 41B3 and mAb 51B3), directed against hen's egg ovomucoid (OM) and different from those we previously reported (mAb 23£5 and mAb 32A8), were prepared and purified. A competitive radioimmunoassay using 12sI_labeled OM showed that both mAb 41B3 and mAb 51B3 could bind all three homologous domains (domains I (DI), II (DII) and III (DIll)) of OM and that they reacted most efficiently with DIll. To analyze the paratope specificities of these four mAbs, a sandwich assay and a competitive radioimmunoassay were done. Only the pair mAb 41 B3 and mAb 51 B3 could not simultaneously bind the OM or domains in the sandwich assay. Only mAb 41B3 inhibited the binding of mAb 51B3 to antigens and vice versa in the competitive radioimmunoassay. These results suggest that mAb 41B3 and mAb 51B3 recognized a closely related site distinct from the epitopes for mAb 23£5 or mAb 32A8. These mAbs may be useful for general studies on epitopes of protein antigens as well as for analyses of the antigenic determinants of OM.

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Section: Comparison Of Four Distinct Idiotypes Of Monoclonal Antibodimentioning

confidence: 99%

Comparison of Four Distinct Idiotypes of Monoclonal Antibodies against Hen’s Egg Ovomucoid

Enomoto

Aoki

Kurisaki

et al. 1987

Agricultural and Biological Chemistry

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“…Each domain is cross-linked by three intradomain disulfide bonds; however, they lack any interdomain disulfide bonds (7). This unique structural characteristic (compared with other egg-white proteins) might explain the higher stability of ovomucoid against digestion with proteinase (8) and heat (9), as well as its strong allergenicity (10,11). Our previous work has shown that there is significantly more human IgG and IgE binding activity to the third domain (DIII) than to the first (DI) and second (DII) domains of ovomucoid in sera derived from egg-allergic patients (12).…”

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IgE Binding Properties of the Recombinant Ovomucoid Third Domain Expressed in Escherichia coli

Sasaki

Mine

2001

Biochemical and Biophysical Research Communications

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The allergenicity of ovomucoid and the effect of its elimination from hen's egg white

Mine

Zhang

2001

J Sci Food Agric

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In order to remove the ovomucoid from hen's egg white, chitin and hydrazide polystyrene beads were used as af®nity ligands with 8.9 and 7.1 mg trypsin g À1 ligand respectively. Ovomucoid was successfully depleted using the trypsin af®nity column without hydrolysation of the other egg white constituents. The components of the egg white were puri®ed by high-performance liquid chromatography, and then the allergenicity of each of these components was compared with that of pooled human serum derived from patients who are allergic to hen's eggs. The importance of using pure protein for studies of the allergenicity of egg white is highlighted, and it was determined (using an enzyme-immunosorbent assay) that ovomucoid and ovalbumin are major allergenic proteins in egg white. The ovomucoid-eliminated egg white preparation exhibited signi®cantly less IgE-binding activity than normal egg white. The ovomucoid-speci®c IgE antibodies may have important implications with regard to the egg-allergic reaction in humans.

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Studies on the Atopic Allergen in Hen's Egg

Cited by 35 publications

References 6 publications

Comparison of Four Distinct Idiotypes of Monoclonal Antibodies against Hen’s Egg Ovomucoid

Comparison of Four Distinct Idiotypes of Monoclonal Antibodies against Hen’s Egg Ovomucoid

IgE Binding Properties of the Recombinant Ovomucoid Third Domain Expressed in Escherichia coli

The allergenicity of ovomucoid and the effect of its elimination from hen's egg white

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