|Select ||PubMed ID ||Description |
|6601671|| J Allergy Clin Immunol. 1983 May;71(5):481-6.|
Immunochemical identification of the allergens in egg white.
The allergenic activities of egg white components were tested by
radioimmunoelectrophoresis (RIEP) and RAST with highly purified proteins. Sera
from 33 patients who reacted to egg ingestion were used for both methods.
Ovalbumin and ovomucoid were shown to be strong allergens by both techniques.
Patients varied in relative reactivity to these two allergens. Conalbumin was
found to be an important allergen by RAST, but its activity was underestimated by
RIEP. Lysozyme was only a weak allergen. Two sera reacted by RIEP with other
neutral egg white components. Both ovalbumin and ovomucoid were found in hard-
and soft-boiled egg white in immunologically recognizable form, and small amounts
of conalbumin were also detectable in cooked egg. There was no significant
association of pattern of reactivity with age, sex, or presence of eczema. The
sera of patients who experienced gastrointestinal symptoms from ingestion of egg
white were less reactive with ovomucoid than sera from patients with other
PMID: 6601671 [Indexed for MEDLINE]
Int Arch Allergy Appl Immunol. 1987;84(3):228-32.
Allergenic cross-reactivity of egg-white and egg-yolk proteins. An in vitro
Walsh BJ(1), Elliott C, Baker RS, Barnett D, Burley RW, Hill DJ, Howden ME.
|3356225|| Epidemiol Infect. 1988 Apr;100(2):291-9.|
Serological examination of IgE- and IgG-specific antibodies to egg protein during
influenza virus immunization.
Yamane N(1), Uemura H.
|2416695|| Int Arch Allergy Appl Immunol. 1986;79(1):101-7.|
Antigenic and allergenic determinants of ovalbumin. I. Peptide mapping, cleavage
at the methionyl peptide bonds and enzymic hydrolysis of native and carboxymethyl
Elsayed S, Hammer AS, Kalvenes MB, Florvaag E, Apold J, Vik H.
The effects of enzymic cleavage and perturbing the conformation of the allergenic
and antigenic determinants of hens egg white albumin (OA) were examined. Hens egg
white extract of a total protein concentration 8.43 g/l was prepared. Isoelectric
focusing in sodium dodecyl sulfate and polyacrylamide gel peptide maps for the
crude egg white extract showed 26 spots visualized by staining with Coomassie
blue. The OA was purified using a TSK-2000 gel filtration chromatography column.
The specific allergenic reactivity of the purified OA as measured by RAST
inhibition and direct RAST was relatively high: 3 micrograms gave an inhibition
of approximately 10%. The cleavage of OA with cyanogen bromide resulted in 4
fractions, all capable of binding specific IgE with the first peak showing the
highest inhibition. Thermal denaturation of OA had no direct effect on the
antigenic reactivity. RAST inhibition values for the denatured protein were
similar to those of the native protein. Carboxymethylation of OA gave a product
with only 20% of the inhibition reactivity. Further treatment with trypsin did
not abolish the allergenic and antigenic reactivities as shown by RAST inhibition
and by deflection of OA line in rocket line immunoelectrophoresis. On the other
hand, limited pepsin hydrolysis destroyed the antigenic structure of the
molecule. The reactivity of OA is thus relatively stable and could easily be
retained making it possible to identify the allergenic determinants of enzymic
hydrolysates used for elucidating the antigenic structure of the molecule.
PMID: 2416695 [Indexed for MEDLINE]
Allergy. 1996 Jan;51(1):8-15.
Monomeric chemically modified allergens: immunologic and physicochemical
Mistrello G(1), Brenna O, Roncarolo D, Zanoni D, Gentili M, Falagiani P.
|9404088|| Arerugi. 1997 Oct;46(10):1007-12.|
[Assessment of allergenic activity of heated and ovomucoid-depleted egg white].
[Article in Japanese]
Wada E(1), Urisu A, Morita Y, Ando H, Yasaki T, Yamada K, Goto M, Wakamatsu T.
|10858989|| Allergy. 2000 Jun;55(6):565-9.|
IgE-binding activity to enzyme-digested ovomucoid distinguishes between patients
with contact urticaria to egg with and without overt symptoms on ingestion.
Yamada K(1), Urisu A, Kakami M, Koyama H, Tokuda R, Wada E, Kondo Y, Ando H,
Morita Y, Torii S.