• Journal of Radiation Protection and Research
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• v.22 no.1
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• pp.23-27
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• 1997

Radiation effects on carbohydrate moiety of chicken ovomucoid, a protease inhibitor as a typical allergenic glycoprotein of egg white, was observed. The trypsin inhibitory activity of chicken ovomucoid decreased exponentially and the inactivation was more significant irradiated in $N_2$ than in $O_2$. From the protein blotting, radiation caused protein degradation in $O_2$ and protein aggregation also in $N_2$. The patterns of carbohydrate blotting were also similar with that of protein blotting. Sugar chains in low molecular weight fraction (MW<5,000) were released by radiation and those in $O_2$ were higher than in $N_2$. From the HPLC patterns of the degradation of sugar chains, all peaks of oligosaccharides have the tendency to decrease with the increase of radiation dose and more remarkable in $O_2$ than in $N_2$. These results suggest that ionising radiation could cause the overall conformational changes of ovomucoid by the degradation and release of oligosaccharides.

• Korean Journal of Food Science and Technology
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• v.36 no.1
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• pp.147-151
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• 2004

Antigenicities of ovomucoid (OM) and ovalbumin (OA) in chicken egg white (EW) before and after NaOH, heat, and pretense treatments were examined by competitive indirect enzyme-linked immunosorbent assay (ciELISA), using rabbit anti-OM and-OA antibodies, Enzymatic hydrolysis of EW did not effectively reduce antigenicity of OM, whereas that of OA was decreased to 1/5,000-1/100,000 by treatment of plant-derived or microbial pretenses. Heat treatment below $100^{\circ}C$ for 30min did not decrease antigenicity of OM, whereas that of OA in heated EW increased maximally to 100 times, Antigenicity of OM in EW effectively decreased by NaOH treatment, disappearing at over 1% NaOH, whereas that of OA increased. Additional heat treatment of NaOH-treated EW at $70^{\circ}C$ for 15min slightly reduced antigenicities of OM and OA.

• BMB Reports
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• v.29 no.4
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• pp.380-385
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• 1996

Ovomucoid third domain is a serine proteinase inhibitor protein which consists of 56 amino acid residues. A fifty picosecond molecular dynamics (MD) simulation was carried out for ovomucoid third domain protein with 5 $\AA$ layer of water molecules. A comparison of main chain atoms in the MD averaged structure with the crystal structure showed that most of the backbone structures are maintained during the simulation. Investigation of the intramolecular hydrogen bondings indicated that most of the interactions between main chain atoms were conserved, whereas those between side chains were reorganized for the period of the simulation. Especially, the side chain interactions around the scissile bond of reactive site P1 (Met18) were found to be more extensive for the MD structures. During the simulation, hydrogen bonds were maintained between the side chains of Glu19 and Arg21 as well as those of Thr17 and Glu19. Extensive side chain interactions observed in the MD structures may shed light on the question of why protein proteinase inhibitors are strong inhibitors for proteinases rather than good substrates.

• Molecules and Cells
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• v.27 no.6
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• pp.657-665
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• 2009

The ovomucoid pre-mRNA has been folded into mini-hairpins adaptable for the RNA recognition motif (RRM) protein binding. The number of mini-hairpins were 372 for pre-mRNA and 83-86 for mature mRNA. The spatial arrangements are, in average, 16 nucleotides per mini-hairpin which includes 7 nt in the stem, 5.6 nt in the loop and 3.7 nt in the inter-hairpin spacer. The constitutive splicing system of ovomucoid-pre-mRNA is characterized by preferred order of intron removal of 5/6 > 7/4 > 2/1 > 3. The 5' splice sites (5'SS), branch point sequences (BPS) and 3' splice sites (3'SS) were identified and free energies involved have been estimated in 7 splice sites. Thermodynamic barriers for splice sites from the least (|lowest| -Kcal) were 5, 4, 7, 6, 2, 1, and 3; i.e., -18.7 Kcal, -20.2 Kcal, -21.0 Kcal, -24.0 Kcal, - 25.4 Kcal, -26.4 Kcal and -28.2 Kcal respectively. These are parallel to the kinetic data of splicing order reported in the literature. As a result, the preferred order of intron removals can be described by a consideration of free energy changes involved in the spliceosomal assembly pathway. This finding is consistent with the validity of hnRNP formation mechanisms in previous reports.

• Preventive Nutrition and Food Science
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• v.7 no.1
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• pp.52-56
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• 2002

This study was conducted to evaluate the possibility of gamma radiation for reducing egg allergies through the observation of conformational and allergenic changes of egg ovomucoid (OM) in basic pH conditions. An OM solution of 2.0 mg/mL was individually prepared with different pH conditions, pH 7.0, 9.0 or 10.0, and was irradiated with the absorbed dose of 10 kGy. Irradiated OM solutions were tested by Ci-ELISA formatted with egg-hypersensitive patients'IgE. Binding abilities of IgE to OM in irradiated solution decreased with the increase of pH. Turbidity of the solution highly increased by irradiation and the increase of pH. A yellowish color was observed in the irradiated OM solution of basic condition. Coagulation of OM by irradiation decreased with the increase of pH, when observed by SDS-PAGE.

• Proceedings of the Acoustical Society of Korea Conference
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• 1998.06d
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• pp.29-34
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• 1998

Egg white의 gel화에 따른 음속과 흡수의 변화가 60와 75$^{\circ}C$에서 크게 나타난 것이 egg white의 어느 단백질 성분에 의한 것인가를 조사하기 위해 egg white의 주요한 단백질 성분인 obalbumin, conalbumin, ovomucoid protein에 대해 gel화에 따른 음속 및 흡수의 변화를 온도 10-95$^{\circ}C$의 범위에서 초음파pulse법을 사용하여 측정하였다. Ovalbumin는 7$0^{\circ}C$, conalbumin는 5$0^{\circ}C$에서 gel화가 시작되었고 ovomucoid는 측정온도범위내에서는 gel화가 진행되지 않았다. Gel화하는 이상의 온도에서 음속과 흡수에 대하여 aging측정을 행하여 gel화에 의한 dam속과 흡수의 변화를 관측하였다. 그 결과 conalbumin는 5$0^{\circ}C$, ovalbumin는 75$^{\circ}C$에서 음속과 흡수의변화가 많이 일어났다. Egg white의 60와 75$^{\circ}C$의 gel화에 의한 음속과 흡수의 큰 변화는 각각 conalbumin과 ovalbumin에 의한 것임을 알았고 Conalbumin과 ovalbumin는 aging 온도를 parameter로하여 이력현상이 관측되었다.

• Proceedings of the Korean Nutrition Society Conference
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• 2001.05a
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• pp.201.2-201
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• 2001

• Korean Journal of Food Science and Technology
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• v.40 no.3
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• pp.343-348
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• 2008

The ovomucoid (OM) of egg whites is recognized as a major allergen. Here, the allergenicity of OM in egg whites (EW) treated by chemical, enzymatic, and physiological methods were investigated by competitive inhibitory ELISA using human IgE antibody acquired from egg-allergic patients. Enzymatic hydrolysis, irradiation, and succinic anhydride treatments did not reduce the allergenicity of the OM effectively. Allergenicity was reduced to only 1/20 by deglycosylation with trifluoromethanesulfonic acid (TFMS). Heat treatment of the OM at $121^{\circ}C$ for 10 min reduced allergenicity to 1/100. Furthermore, NaOH (over 3%) treatment reduced allergenicity to 1/10,000, and the combinatory treatment of NaOH (over 0.3%) and heat ($70^{\circ}C$, 15 min) reduced it to less than 1/10,000, which was the most effective method. In this study, which analyzed treated EW using ELISA and patient-derived IgE, the OM allergenicity was nearly the same as its antigenicity according to ELISA using rabbit IgG. However, in the case of the TFMS-treated EW, the antigenicity was much lower than the allergenicity. These results suggest that the allergenicity of OM is slightly different from its antigenicity.

• Food Science of Animal Resources
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• v.30 no.1
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• pp.36-41
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• 2010

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. Cross-reactivity 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 ($mean{\pm}SD$) were $129{\pm}13.7%$, $73.9{\pm}12.5%$, and $65.5{\pm}13.6%$, 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.

• Journal of Nutrition and Health
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• v.27 no.10
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• pp.979-987
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• 1994

We have examined the antigen specificity in orally tolerant mice fed with the casein(CN) diet. In contrast to previous reported results of studies on oral tolerance, these mice responded poorly to ovalbumin(OVA) and ovomucoid(OM), as well as $\alpha$sl-enriched fraction of these cells suppressed anti $\alpha$sl-CN antibody production of naive mice, but could not significantly suppressed antibody response of previously immunized recipient mice. These results indicate that oral tolerance was not medicate through suppressor T cell activities.