Hen's Egg Protein Research Articles

Baked Egg Oral Immunotherapy: Current State in Pediatric Age.

Hen's egg allergy is one of the most common food allergies in the Western world, with an increase in recent years. It affects about 9.5% of the pediatric population, and the onset most often occurs before the first year of life. The occurrence of spontaneous oral tolerance acquisition varies among studies, but it is generally high by school age. Nowadays, allergen immunotherapy may represent the only therapeutic strategy able to modify the natural history of hen's egg allergy. Specifically, many children with hen's egg allergy may tolerate baked eggs. Food processing, specifically high temperatures, alters the allergenicity of hen's egg proteins by causing conformational changes in allergen epitopes, which makes them less allergenic. This review aims to discuss the scientific evidence in the field of baked egg oral immunotherapy in hen's egg-allergic children, with a meticulous examination of the pertinent literature surrounding the subject matter.

Taste characteristics and umami mechanism of novel umami peptides from hen egg proteins

The study aimed to identify umami peptides from the hen egg proteins including ovotransferrin, ovalbumin, ovomucoid, and ovomucin using virtual enzymatic, molecular docking, electronic tongue analysis, and molecular dynamic simulation. The results showed that the interaction energy of DDNK, DLTK, and EHGK with the umami receptor T1R1/T1R3 was −124.3, −109.7, and −107.4 kcal/mol, respectively. The umami values for peptides DDNK, DLTK, and EHGK were 3.02 ± 0.33, 3.35 ± 0.24, and 4.19 ± 0.21, respectively, measured at the concentration of 0.1 mg/mL by electronic tongue. Molecular docking analysis indicated that residues Glu70, Gln278, and Asp147 might be the key amino acids within the T1R1/T1R3 binding site. Besides, molecular dynamics simulation revealed that the T1R1/T1R3 formed stable complexes with the umami peptides during the simulation. The work indicated that DDNK, DLTK, and EHGK may potentially serve as a good source of desirable umami peptides and can be used as the precursor of flavoring agent.

Repression Effects of Hydrolysates from Hen-Egg Proteins on Amyloid Fibril Formation.

Amyloid fibrils, which are formed from aggregates of aberrant proteins, can cause various forms of amyloidosis (including Alzheimer's disease). Such disorders often occur in elderly populations and are suspected to be lifestyle related. Thus, it has been speculated that some foodstuffs could be beneficial for preventing amyloidosis. In this study, we determine whether fibril formation by the hen egg white lysozyme (HEWL) could be inhibited by conducting a thioflavin T assay followed by fluorescence and electron microscopy observations. The results demonstrated that four peptide specimens prepared by the hydrolysis of crude proteins from the egg white, egg yolk, chalazae, and eggshell membrane of hen eggs effectively inhibited HEWL fibril formation. Among the four specimens, peptides from chalazae exhibited the highest preventive ability. The superiority of chalaza peptides was also observed when fibril formation was assayed using a full-length human lysozyme and human amyloid β peptide 1-42, which is the key factor for the development of Alzheimer's disease. Our study of the fibrillization of the human lysozyme also showed that metal ions (Zn2+, Ca2+, Co2+, Mn2+ and Al3+) promoted fibrillization, and their effects were abolished by the peptide specimens (especially by chalaza peptides). Thus, we conclude that chicken-egg proteins could be a convenient source of therapeutic materials for amyloidosis.

Vaccine Additives and Residuals

Vaccines contain active ingredients (antigens; mRNA) and inactive ingredients (stabilizers, antimicrobials, inactivating agents, antibiotics, residues of production). Formaldehyde is a “natural substance” in human metabolism. With this “natural presence” in mind, the amount of formaldehyde contained in vaccines is not relevant. However, high formaldehyde concentrations in gaseous form may act as a carcinogen. Thiomersal was withdrawn from inactivated pediatric vaccines from the year 2000. Available evidence today indicates that it does not cause autism. It has never been an ingredient in life vaccines. Penicillin and streptomycin are not used or added during vaccine production, allergies to neomycin are extremely rare. Patients with severe hen egg protein allergy (1) can safely be vaccinated with MMR- or TBE-vaccines; (2) should receive egg-protein-free influenza vaccine based on cell culture technology; (3) Yellow fever vaccine is contraindicated, but if necessary, it can be given in graded doses by an allergist.

Copper-Free Click Enabled Triazabutadiene for Bioorthogonal Protein Functionalization.

Aryl diazonium ions have long been used in bioconjugation due to their reactivity toward electron-rich aryl residues, such as tyrosine. However, their utility in biological systems has been restricted due to the requirement of harsh conditions for their generation in situ, as well as limited hydrolytic stability. Previous work describing a scaffold known as triazabutadiene (TBD) has shown the ability to protect aryl diazonium ions allowing for increased synthetic utility, as well as triggered release under biologically relevant conditions. Herein, we describe the synthesis and application of a novel TBD, capable of installation of a cyclooctyne on protein surfaces for later use of copper-free click reactions involving functional azides. The probe shows efficient protein labeling across a wide pH range that can be accomplished in a convenient and timely manner. Orthogonality of the cyclooctyne modification was showcased by labeling a model protein in the presence of hen egg proteins, using an azide-containing fluorophore. We further confirmed that the azobenzene modification can be cleaved using sodium dithionite treatment.

Aminopeptidase N inhibitory peptides derived from hen eggs: Virtual screening, inhibitory activity, and action mechanisms

Aminopeptidase N (APN) is an important zinc-dependent metalloproteinase expressed on cell surfaces. This study was done to find APN inhibitory peptides using virtual screening and molecular docking. Hen egg proteins were cleaved using pepsin and trypsin in silico to peptides of different lengths. Dipeptides and tripeptides are more easily absorbed in the gastrointestinal tract (GIT). The bioactivity, solubility, absorption, distribution, metabolism, excretion, and toxicity properties of the dipeptides and tripeptides were then predicted. APN was used as a molecular docking target for potential peptides. The tripeptides CNR, CDR and GEF were docked with the APN residues, His388, His392, Glu411, Glu355 and Tyr477. An in vitro APN inhibition assay showed that the IC50 values of CNR, CDR and GEF against APN were 8.94, 6.42, and 61.7 mM, respectively.

Gene Expression Profiling in Ovaries and Association Analyses Reveal HEP21 as a Candidate Gene for Sexual Maturity in Chickens.

Simple SummaryChicken meat and egg productions are essential for human beings. Sexual maturity is important for both egg production and meat flavor. It is necessary to elucidate the genetic mechanism of chicken sexual maturity. In current study, we used digital gene expression (DGE) RNA-sequencing analysis to investigate differential expression of genes in pre-pubertal and post-pubertal ovaries in two different sub-breeds of chicken with different onsets of sexual maturity. After the analysis of RNA-sequencing data, numerous differentially expressed genes were found in both comparisons (32 day old, early-sexual-maturity pre-laying hens (P-F-O1) vs. 103 day old early-sexual-maturity laying hens (P-F-O2), and 32 day old late-sexual-maturity pre-laying hens (L-F-O1) vs. 153 day old late-sexual-maturity pre-laying hens (L-F-O2)). With the bioinformatic analysis, hen egg protein 21 kDa (HEP21) was chosen as the candidate gene to conduct following experiment. The variations in HEP21 were screened and association analyses between rs315156783 and reproductive traits were investigated in fifth-generation Ningdu Yellow chickens from a closely bred population. These results demonstrated that HEP21 is a candidate gene for sexual maturity and ovary development in chickens. However, the underlying mechanism of how HEP21 regulates chicken sexual maturity needs further focused studies.The age of onset of sexual maturity is an important reproductive trait in chickens. In this study, we explored candidate genes associated with sexual maturity and ovary development in chickens. We performed DGE RNA-sequencing analyses of ovaries of pre-laying (P-F-O1, L-F-O1) and laying (P-F-O2, L-F-O2) hens of two sub-breeds of Ningdu Yellow chicken. A total of 3197 genes were identified in the two comparisons, and 966 and 1860 genes were detected exclusively in comparisons of P-F-O1 vs. P-F-O2 and L-F-O1 vs. L-F-O2, respectively. Gene ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses showed that genes involved in transmembrane signaling receptor activity, cell adhesion, developmental processes, the neuroactive ligand–receptor interaction pathway, and the calcium signaling pathway were enriched in both comparisons. Genes on these pathways, including growth hormone (GH), integrin subunit beta 3 (ITGB3), thyroid stimulating hormone subunit beta (TSHB), prolactin (PRL), and transforming growth factor beta 3 (TGFB3), play indispensable roles in sexual maturity. As a gene unique to poultry, hen egg protein 21 kDa (HEP21) was chosen as the candidate gene. Differential expression and association analyses were performed. RNA-seq data and qPCR showed that HEP21 was significantly differentially expressed in pre-pubertal and pubertal ovaries. A total of 23 variations were detected in HEP21. Association analyses of single nucleotide polymorphisms (SNPs) in HEP21 and reproductive traits showed that rs315156783 was significantly related to comb height at 84 and 91 days. These results indicate that HEP21 is a candidate gene for sexual maturity in chickens. Our results contribute to a more comprehensive understanding of sexual maturity and reproduction in chickens.

Effect of storage time on the quality of smoked Oreochromis niloticus

Effect of storage time on the quality of smoked Oreochromis nilotius was studied. One hundred fish samples of O. niloticus (average weight 210 ± 15g) was used. Analysis carried out include: proximate, mineral composition (Ca, Na, Fe and Mg), biochemical, amino acid and sensory evaluation. Data obtained was subjected to Analysis of Variance (ANOVA) while the sensory data was subjected to nonparametric test (Kruskal Wallis test). Proximate quality, mineral, amino acid, biochemical and sensory quality of frozen O. niloticus content reduced with increase in storage period. Na and Mg were the most abundant mineral while glutamic acid and lysine were the most concentrated non-essential amino acid (NEEA) and essential amino acid (EAA) respectively. The total volatile base nitrogen (TVBN), trimethyl amine (TMA) and peroxide values (PV) obtained are within the recommended level for good quality food while NEAA and EAA are within recommended values by WHO. The amino acid scores of the fish in relation to the amino acid scoring pattern of whole hen's egg protein indicate that lysine had the highest amino acid score. No significant (χ2= 6.624, p > 0.05) variation was observed in the score allotted for the flavor of smoked O. niloticus during storage. Smoked O. niloticus being a good source of protein, minerals and amino acids, and the quality is within good quality protein recommended by world health organization (WHO), is therefore recommended for consumption.

Novel membrane peptidase inhibitory peptides with activity against angiotensin converting enzyme and dipeptidyl peptidase IV identified from hen eggs

Abstract Angiotensin converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) are important membrane peptidases. The inhibition of ACE and DPP-IV enzymes has become a key therapeutic target for the treatment of hypertension and diabetes. This study was conducted to discover membrane peptidase inhibitory peptides that inhibit ACE and DPP-IV. Egg proteins were cleaved by pepsin and trypsin in silico. The potential activity, solubility, absorption, distribution, metabolism, excretion, and toxicity of the peptides were then predicted online. Finally, ACE and DPP-IV were applied as molecular docking targets for the potential peptides. After simulating gastrointestinal digestion, the IC50 values of ADF, MIR, and FGR against ACE activity were 27.75 ± 0.90 mM, 24.97 ± 0.80 mM, and 66.98 ± 1.40 μM, against DPP-IV activity were 16.83 mM, 4.86 mM, and 46.22 mM, respectively. The ACE and DPP-IV inhibitory peptides identified from hen egg proteins can be used as functional food ingredients for controlling hypertension and diabetes.

Ileal digestibility of intrinsically labeled hen's egg and meat protein determined with the dual stable isotope tracer method in Indian adults

ABSTRACTBackgroundProtein quality assessment through the Digestible Indispensable Amino Acid Score requires accurate measurements of true ileal protein and amino acid digestibility, for which a dual isotope technique was recently developed. However, the ileal digestibility of indispensable amino acids (IAA) in humans from high-quality proteins is not well known.ObjectiveThe aim of this study was to intrinsically label hen's egg and meat protein by the use of uniformly 2H-labeled amino acids, and to measure their true ileal indispensable amino acid (IAA) digestibility via the dual isotope method in humans.Design 2H-labeled lyophilized boiled egg white protein, whole boiled egg, and cooked meat were obtained from layer hens (BV-300) administered a uniformly 2H-labeled amino acid mix orally for 35 d with their daily feed. The ileal IAA digestibility of these proteins was determined with reference to digestibility of previously characterized [U-13C]spirulina in a dual tracer method in healthy Indian subjects whose intestinal health was measured by the plasma kynurenine-to-tryptophan (KT) ratio.ResultsAll subjects had normal KT ratios. The mean ± SD true ileal IAA digestibility of 2H-labeled egg white protein, whole boiled egg, and cooked meat was 86.3% ± 4.6%, 89.4% ± 4.5%, and 92.0% ± 2.8%, respectively. Leucine digestibility correlated with the KT ratio (r = −0.772; P = 0.009).ConclusionsUniformly 2H-labeled hen's egg and meat protein can be used to measure ileal IAA digestibility by the dual isotope tracer approach in humans. The mean IAA digestibility values for these high-quality proteins in the healthy Indians studied were similar to values obtained in earlier human and animal experiments. Leucine digestibility in these meal matrices correlated with the KT ratio, but this aspect needs further evaluation. This trial was registered at the Clinical Trials Registry of India (http://ctri.nic.in) as CTRI/2018/03/012265.

Early-life sensitization to hen's egg predicts asthma and rhinoconjunctivitis at 14years of age.

Sensitization to both inhalant and food allergens has been shown to be risk factors for development of asthma and rhinoconjunctivitis (RC). However, few studies have addressed the role of transient or persistent IgE sensitization to specific allergens in early life for later development of allergic diseases. The aim of this study was to explore the association between transient and persistent sensitization in early life and the development of asthma and RC at 6 and 14years. The Danish Allergy Research Center (DARC) cohort is a prospective non-interventional birth cohort study comprising 562 children. For the purpose of this study, we examined a subgroup of the original cohort with specific IgE measured at, at least 3 of 4 follow-ups between 3 and 18months of age (n=366). Multiple logistic regression models were used to investigate the association between transient and persistent early-life sensitization to groups of and to individual allergens and asthma and RC at 6 and 14years compared to a reference group with no sensitization. Both transient early-life sensitization and persistent early-life sensitization to cow's milk or hen's egg proteins were associated with asthma (aOR 3.99[1.41-11.32] and 5.95[1.78-19.92]) and RC (aOR 2.94[1.19-7.28] and 6.18[1.86-20.53]) at 14years, this association being driven mainly by sensitization to hen's egg. Transient early-life sensitization to house dust mite (HDM) had increased risk of asthma (aOR 3.80[1.17-12.41]) at 14years. Early transient IgE sensitization and persistent IgE sensitization to hen's egg were associated with asthma and RC at 14years. Furthermore, sensitization to HDM was associated with asthma at 14years.

Hen's egg allergen in house and bed dust is significantly increased after hen's egg consumption-A pilot study.

Environmental exposure to food allergens may be a risk factor for cutaneous sensitization. Previous studies could detect peanut allergen in house dust. In this pilot study, we wanted to investigate whether hen's egg allergen is detectable in house dust collected from different household areas and whether levels are increased after intentional hen's egg consumption. Hen's egg protein levels of dust samples were measured using ELISA. In 8 of 8 households, hen's egg was detectable in dust samples of eating area and bed. Forty-eight hours after intentional hen's egg consumption, hen's egg protein levels were significantly increased in both. Still, further research is necessary to investigate whether hen's egg allergen in house and bed dust plays a role in sensitization via skin.

Probiotics in the prevention of eczema: a randomised controlled trial

ObjectiveTo evaluate a multistrain, high-dose probiotic in the prevention of eczema.DesignA randomised, double-blind, placebo-controlled, parallel group trial.SettingsAntenatal clinics, research clinic, children at home.PatientsPregnant women and their infants.InterventionsWomen from 36 weeks...

Pivotal roles for hormonally regulated expression of the HEP21 gene in the reproductive tract of chickens for oviduct development and in ovarian carcinogenesis

Hen egg protein (HEP21) is a 21-kDa secreted protein and has a single copy of the Ly6/uPAR domain. Although HEP21 is expressed primarily in the chicken oviduct, its biological function(s) in the reproductive system of chickens is not known. Thus, in the present study, we investigated expression patterns of HEP21 with respect to hormonal regulation, oviduct development, changes in expression in laying hens undergoing induced molting, and in the development of ovarian carcinogenesis in laying hens. Results of present study indicated that HEP21 messenger RNA (mRNA) expression increased (P < 0.001) in the chicken oviduct in response to estrogen. In situ hybridization analyses revealed expression of HEP21 mRNA predominantly in glandular (GE) and luminal epithelia of the magnum of the chicken oviduct in response to estrogen. The expression of HEP21 mRNA decreased (P < 0.001) as the oviduct regressed during induced molting and increased (P < 0.001) with recrudescence of the oviduct following molting. HEP21 mRNA was most abundant in GE of the oviduct during recrudescence, but not during oviduct regression following induced molting. Moreover, we found abundant expression of HEP21 in GE of cancerous ovaries, but not in normal ovaries of hens. Collectively, results of present study suggest that HEP21 is an estrogen-responsive gene in the oviduct of hens that likely regulates development of the chicken oviduct, and egg production and formation. Furthermore, there is increased expression of HEP21 in epithelial-derived ovarian cancer suggesting that HEP21 could be used for diagnosis and monitoring carcinogenesis in laying hens and in women.

Oral food desensitization in children with IgE‐mediated hen’s egg allergy: a new protocol with raw hen’s egg

Hen's egg allergy affects young children and can cause severe allergic reactions. Avoidance results in dietary limitations and can affect the quality of life, especially in cases where potentially life-threatening reactions exist. Our objective was to desensitize children with moderate-severe IgE-mediated hen's egg allergy over a 6-month period, by introducing increasing and very gradual daily doses of raw hen's egg in order to enable the children to assume 25ml of this food, or to induce tolerance to the highest possible dose. The protocol foresaw the egg reintroduction in the home setting. In this randomized, controlled open study, 20 hen's egg allergic children (10 in the active group) were admitted. A convincing history or a positive double-blind placebo-controlled food challenge confirmed the diagnosis. Oral desensitization was performed with increasing doses starting from 0.27 mg of hen's egg proteins (1 drop of raw hen's egg diluted 1:100). We adopted an original, mathematically calculated protocol in order to ensure a constant, daily increment of doses. 8/10 children (80%) in the active group achieved the daily intake of 25ml over a 6-month period. One child (10%) could tolerate up to 2ml/day while another child (10%) failed the desensitization. Six months after enrolment only 2 children in the control group (20%) could tolerate hen's egg. We successfully desensitized 8/10 children with IgE-mediated hen's egg allergy in a 6-month period. The partial outcome in the child who could tolerate 2ml/day reduced the risk of severe reactions after unnoticed introduction of egg. A regular protocol that ensures a daily constant increase of doses helps to reduce possible adverse events, thus improving safety and effectiveness.

Preparation of a genipin blue from egg protein and genipin

Genipin blue is a pigment prepared from the reaction of genipin with amino acid. We describe herein a new method used to prepare genipin blue, water-soluble blue pigments, through the reaction of hen egg protein with genipin. The effects of reaction time, reaction temperature, the pH value of the solution and the mass ratio of the reactants on the preparation are studied. One part of genipin reacted with eight parts of hen egg protein (w/w) in water (pH value of reaction system 7.5) at 60°C for 96 h and gave blue pigments with the maximum colour value of 146.2. The blue pigments showed identical absorption activity in UV spectroscopy (λ max = 584 nm) to that of gardenia blue pigments, which were prepared from the reaction of genipin with amino acid.

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

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 (<TEX>$mean{\pm}SD$</TEX>) were <TEX>$129{\pm}13.7%$</TEX>, <TEX>$73.9{\pm}12.5%$</TEX>, and <TEX>$65.5{\pm}13.6%$</TEX>, 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.

Comparative Evaluation of the Amino Acid Profile of the Brain and Eyes of Guinea Fowl (Numida meleagris) Hen

The amino acid composition of the brain and eyes of the matured female guinea fowl (Numida meleagris) was determined on a dry weight basis. The total essential amino acids ranged from 38.4-37.5g/100 g crude protein or from 47.5-52.2 % of the total amino acid. The amino acid score showed that lysine ranged from 0.81 - 0.89 (on whole hen's egg comparison), 0.92-1.00 (on provisional essential amino acid scoring pattern) and 0.869 - 0.95 (on suggested require- ment of the essential amino acid of a preschool child). The predicted protein efficiency ratio was 1.82 - 2.33, the essential amino acid index range was 1.11 - 1.45 and the calculated isoelectric point range was 4.64 - 4.32. The correlation coeffi- cient (rxy) was positive and significant at r0.05 for the total amino acids, amino acid scores (on all the comparisons made) and the isoelectric point in the two samples. Results have good comparison with whole hen's egg protein.

Idrabiotaparinux, a Biotinylated Long-Acting Anticoagulant, in the Treatment of Deep Venous Thrombosis (EQUINOX Study): Safety, Efficacy, and Reversibility by Avidin

Idrabiotaparinux is a novel synthetic anticoagulant that links idraparinux, a specific, indirect factor Xa inhibitor, to biotin. The long half-life of idraparinux allows once-weekly (o.w.) subcutaneous (s.c.) injection. Avidin, a hen egg protein, specifically and tightly binds with biotin. When given by intravenous (i.v.) infusion, avidin (half life: 15-minutes) reverses the anti-factor Xa (a-Xa) activity of idrabiotaparinux by forming a complex that is rapidly cleared from the circulation. Idraparinux 2.5 mg s.c. o.w. was effective and safe in the van Gogh DVT trial of 2904 patients with deep vein thrombosis (DVT), when compared with standard anticoagulant therapy 1.Methods: In EQUINOX, patients with symptomatic and confirmed DVT were randomised to receive weekly s.c. injection of equimolar amounts of idrabiotaparinux (3 mg) or idraparinux (2.5 mg) for 6 months. The aims of this multicentre, double-blind, study were to demonstrate, at the end of the 6 months of therapy, bioequipotency of idrabiotaparinux with idraparinux, to measure the effect of i.v. avidin on peak circulating a-Xa activity, and to document efficacy and safety. The main outcome events were clinically relevant bleeding (major or not), death, or symptomatic recurrent venous thromboembolism (VTE) within 6 months of randomisation, assessed by a blinded independent adjudication committee. Reversal of anticoagulant effect by 100 mg i.v. avidin infused over 30 minutes, and its safety, were assessed in a subset of patients re-randomised at 6 months and blindly allocated to receive avidin (idrabiotaparinux arm) or placebo (idrabiotaparinux and idraparinux arms, to preserve blinding). Avidin or placebo was infused 2–5 hours (around tmax) after the last injection of the 6 month treatment period; plasma a-Xa activity was measured just before avidin/placebo infusion, just after, and then for 5 days.Results: Of 757 patients randomised, 385 received idrabiotaparinux and 370 idraparinux. Overall, 22.7% had previous venous thromboembolism (VTE), 5.2% had cancer within the past 6 months, 53.8% had apparently unprovoked thrombosis, and 36.2% were aged >65. There was less clinically relevant bleeding (20 v. 27; 5.2% v. 7.3%) and less major bleeding (3 v. 14; 0.8% v. 3.8%) with idrabiotaparinux than with idraparinux. Rates of recurrent VTE and of fatal or non-fatal pulmonary embolism PE were similar with idrabiotaparinux and idraparinux (VTE: 9 v. 12; 2.3% v. 3.2%. PE: 6 v. 7; 1.6% v. 1.8%). Trough levels of a-Xa activity were identical in the treatment groups throughout 6 months. Of 52 idrabiotaparinux patients re-randomised at 6 months to receive i.v. avidin or placebo, 41 were analysable for reversal of a-Xa activity (23 avidin and 18 placebo). At the end of the 30 minute avidin infusion, mean anti-Xa activity was reduced by 77.8%, sustained for at least 5 days, compared with 2.4% after placebo (p = 3.45 × 10−15). No allergic reactions were observed to avidin.Conclusion: A 6-month treatment period with idrabiotaparinux, compared to idraparinux in patients with DVT, showed a comparable efficacy with a trend to less bleeding. Trough a-Xa activity was identical in the two groups. Avidin infusion at around tmax after the last idrabiotaparinux injection led to rapid and substantial reversal of a-Xa activity, sustained for at least 5 days. Avidin infusion was well-tolerated.

Establishment of a Highly Sensitive Sandwich Enzyme-Linked Immunosorbent Assay Specific for Ovomucoid from Hen’s Egg White

A highly sensitive sandwich enzyme-linked immunosorbent assay (ELISA) kit was established for quantifying ovomucoid from hen's egg white, which has been considered as one of the major allergen in egg white. The detection limit reached 0.041 ng/mL, and linearity ranged from 0.1 to 6.25 ng/mL. Intra- and interassay coefficient variations were all lower than 5% at three concentrations (0.5, 2.5, and 5 ng/mL). No cross-reactivity was observed with bovine serum, horse serum, goat serum, human serum, duck egg white, goose egg white, quail egg white, and pigeon egg white, but a low level of cross-reactivity was found with chicken serum. The ELISA kit was established on the basis of two monoclonal antibodies (mAbs) recognizing different epitopes of ovomucoid. However, these mAbs were generated using commercially purified ovalbumin as immunogen. Studies on the relative allergenicity and antigenicity of egg white protein have been performed by many researchers, but there were controversial opinions reported previously because of the impurity of each egg white protein used in various studies. In the present work we measured the degree of ovomucoid contamination in commercially purified ovalbumin sample, and the value was about 11%. We also determined the ovomucoid residue in influenza vaccine samples for the first time. These data showed that the ELISA kit we established could serve as an effective method for precisely quantifying concentrations of ovomucoid in the egg industry and as a useful tool for the research of allergenicity and antigenicity of hen's egg proteins.