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International audience; To identify apoproteins present in purified low-density lipoproteins from hen egg yolk in relation with their emulsifying properties, they have been separated by SDS-PAGE. We identified two different proteins by liquid chromatography-tandem mass spectrometry analysis of the peptides obtained by the trypsin digestion of protein gel bands. Apovitellenin I was identified as a monomer and a dimer. Its amino acid sequence was totally confirmed, and molecular mass determination by liquid chromatography-mass spectrometry showed that it did not present post-translational modifications but only a slight heterogeneity by the loss of one or two amino acids at the C-terminal part of the protein. Apolipoprotein B was identified into seven bands corresponding to fragments resulting of a processing of the hen blood apo-B protein. The identity of the fragments was determined by the observation of the sequence coverage by trypsin peptides and the sequence alignment with homologous human blood apolipoprotein B-100.

Background Levels of IgE antibody to egg white of greater than 7 kIU/L are highly predictive of clinical reactivity to egg, and lower levels often require evaluation with oral food challenge (OFC) to establish definitive diagnosis. OFCs have inherent risks, and diagnostic criteria indicating high likelihood of passing would be clinically useful. Objective We sought to determine whether the size of the skin prick test (SPT) to egg white adds diagnostic utility for children with low egg white–specific IgE antibody levels. Methods A retrospective analysis of clinical history, egg white–specific IgE antibody levels, SPT responses, and egg OFC outcomes was performed. Results Children who passed (n = 29) egg OFCs and those who failed (n = 45) did not differ significantly in age, clinical characteristics, or egg white–specific IgE levels. There were, however, significant differences between both egg white SPT wheal response size and egg/histamine SPT wheal index. Children who failed egg OFCs had a median wheal of 5.0 mm; those who passed had a median wheal of 3.0 mm ( P = .003). Children who failed egg OFCs had a median egg/histamine index of 1.00; those who passed had a median index of 0.71 ( P = .001). For egg white–specific IgE levels of less than 2.5 kIU/L, an SPT wheal of 3 mm or an egg/histamine index of 0.65 was associated with a 50% chance of passing. Conclusion In children with low egg white–specific IgE levels, those with smaller SPT wheal responses to egg were more likely to pass an egg OFC than those with larger wheal responses. The size of the egg white SPT response might provide additional information to determine the timing of egg OFC. Clinical implications The size of the egg white SPT wheal response might provide the clinician with additional information to determine the timing of egg OFC in children with low egg white–specific IgE antibody levels.

Embryos of the blue crab Callinectes sapidus develop in egg sacs carried on the abdomen of the female. They develop over a period of 10-13 days at 28 degrees C and are nutritionally dependent on yolk until they emerge from the egg sacs as free-swimming zoeae. The principal component of blue crab yolk is lipovitellin (LpII), a water-soluble lipoprotein composed of approximately equal amounts of lipid and protein. We followed changes in the concentration of apoproteins of LpII during embryogenesis by ELISA and Western blots, using monoclonal antibodies against two LpII apoprotein associated peptides identified as Protein A (107 kDa) and Protein B (75 kDa). During embryogenesis there was a decrease in Protein B but an increase in two smaller peptides (52 and 35 kDa) that reacted with the Protein B antibody. Utilization of LpII during embryogenesis was also followed morphologically by immunohistochemistry. Utilization of LpII was slow in early embryonic stages, followed by rapid utilization in late embryonic stages, such that only traces of LpII were present at the end of embryogenesis. The cells of the developing hepatopancreas appear to play an important role in the utilization of LpII.

Egg is one of the 5 major allergenic foods that are responsible for more than 3/4 of food allergies in children. Food-allergic responses can be controlled by avoidance of the offending foods. The applicability of a commercial enzyme-linked immunosorbent assay (ELISA) kit for the detection of egg in food products such as cookies, crackers, pretzels, salad dressings, and raw and cooked noodles was evaluated. A preliminary evaluation of an antibody-based biosensor was also performed. A National Institute of Standards and Technology (NIST) whole dried egg powder reference material, SRM 8415, was used as a standard. A homogeneous and stable aqueous egg suspension was prepared for the evaluation of the performance of the Veratox for Egg Allergen Test (Neogen Corp., Lansing, MI). This test does not detect egg yolk proteins. Each gram of the aqueous dried egg suspension contained 643 microg whole dried egg, 0.5 mg thimerosal, and 2.5 mg bovine serum albumin. When cookies, crackers, salad dressings, noodles, and ice cream were spiked at a level of 24 mg/kg SRM 8415, recoveries for whole egg averaged about 28%. All foods containing egg as indicated on the ingredient label were found positive by the Veratox test. No false positives occurred in samples that did not contain eggs. Similar results were obtained using the Naval Research Laboratory (NRL) array biosensor, an evanescent wave fluoroimmunosensor. Results for cooked noodles showed that they contained1% of the egg found in uncooked noodles. A comparison of extracts from cooked and uncooked noodles by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) revealed differences in protein profiles. The boiling of the noodles could have reduced the immunoreactivity of the egg proteins to the antibodies used in the kit or rendered the egg proteins nonextractable.

Thirty four healthy young volunteers (22 men, 12 women; age 25.7 +/- 5.8 years; BMI 20.8 +/- 2.3 kg/m2) participated in a randomized controlled cross-over trial on the effect of consuming one boiled egg every day for 8 wk on the serum lipid profile. The only significant change after 8 wk of egg consumption was an elevation of the total cholesterol/HDL cholesterol ratio. However, scrutiny of individual responses revealed that twelve of the subjects (10 men, 2 women) had a greater than 15% rise in the LDL cholesterol level after 8 wk of egg consumption. These subjects, considered hyperresponders, showed significant increases (P0.025) at both 4 wk and 8 wk after egg consumption in total cholesterol and LDL cholesterol levels, and at 8 wk in total cholesterol/HDL cholesterol ratio. The remaining 22 hyporesponders showed no change in any of the variables measured at 4 wk or 8 wk after egg consumption. In view of the high nutritional value of eggs, a blanket ban on eggs is not justified. However, since up to one-third of the population may be hyperresponders, knowing the response of an individual is important before making the egg a regular item of the diet.

In the present study we evaluate the blood pressure-lowering effect of the following products: the hydrolysate obtained from egg white (EW) by enzymatic treatment with pepsin (HEW), the peptide fraction of HEW with molecular mass lower than 3000 Da (HEW, This study was supported by an INIA-MCYT project (CAL01-046-02) and an MCYT project (AGL2000-1480)

Egg white protein (EWP) was phosphorylated by dry-heating in the presence of pyrophosphate at pH 3.0-7.0 and 85 degrees C for 1 and 5 days, and the functional properties of the phosphorylated EWP (PP-EWP) were investigated. The phosphorylation was accelerated with a decrease of pH from 7.0 to 3.0 and for heating times from 1 to 5 days. The phosphorus content of EWP increased approximately 1.05% by dry-heating at pH 4.0 and 85 degrees C for 5 days in the presence of pyrophosphate, which was higher than that of casein. The electrophoretic mobility of EWP increased with an increase in the phosphorylation level. The surface hydrophobicity of EWP increased by phosphorylation. The heat stability, emulsifying properties, and digestibility of EWP were improved by phosphorylation. The calcium phosphate-solubilizing ability of EWP was enhanced by phosphorylation. A firmer and transparent heat-induced gel of PP-EWP was obtained, and the water-holding capacity of heat-induced PP-EWP gel was higher that that of the control. These results suggest that phosphorylation by dry-heating in the presence of pyrophosphate is a useful method for improving the functional properties of EWP.

Enzyme-linked immunosorbent assay (ELISA) has been considered extremely useful for the detection of markers of allergenic substances in food, because it is simple, offers a suitable sensitivity, and is useful in providing quantitative results. Allergenic protein present in processed food can be denatured or altered, hindering therefore their possibility to be extracted and detected. This paper reports the development of an ELISA method that can be used for the determination of allergenic proteins in buffer solutions containing SDS, a surfactant, and 2-mercaptoethanol, a reducing agent. Measurement by ELISA in solutions containing 1% SDS and 7% 2-mercaptoethanol has been made possible by using an antibody prepared through immunization with an antigen denatured with SDS and 2-mercaptoethanol. This ELISA technique can be used to measure proteins in food that have been denatured by various manufacturing processes. An example is egg white albumin, which is susceptible to heat denaturation and has been difficult to recover from food in the past. Its recovery was improved 10- to 100-fold by the new ELISA method as compared with previous methods. This means that allergenic substances in food can now be detected quantitatively. This method can be very useful in allergy prevention and control strategies.

The ooplasm of mature oocytes of the polychaete Neanthes arenaceodentata is characteristically filled with yolk platelets. A major component of these structures is lipovitellin, which provides energy and materials required by newly hatched larvae. The lipovitellin isolated and purified from the fertilized eggs of this polychaete was a high-density lipoprotein composed of protein (57%), lipid (42%) and carbohydrate (1%). The lipid component included phospholipids (92% of lipid), triacylglycerol (3% of lipid) and cholesterol (3% of lipid), while sodium dodecyl sulfate-gel electrophoresis showed the major protein component was a 120-kDa peptide. Microscopically, mature oocytes were present in the coelom along with phagocytic eleocytes. The presence of muscle fragments and oil droplets in eleocytes suggests that eleocytes play an important role in providing the protein and lipid needed for the assembly of lipovitellin in the oocytes.

Two lipovitellin (LV) forms containing the same apoproteins but differing in their lipid composition were isolated from Macrobrachium borelii eggs at early (LVe) and late (LVI) embryogenic stages and characterized. These two forms of LV, as well as liposomes prepared with lipids extracted from them, were used as simpler models to study the effect of the pesticide fenitrothion (FS) on their structures and functions. Rotational diffusion and fluorescence lifetime of two fluorescent probes [1,6-diphenyl-1,3,5-hexatriene (DPH) and 3-(p-(6-phenyl)-1,3,5-hexatrienal)phenylpropionic acid (DPH-PA)] were used to obtain information on structural changes induced by FS in the inner and outer regions of the LV, respectively. Comparison of the rotational behavior of these probes in native LV and liposomes (LP) from extracted LV lipids suggests that apoprotein-lipid interactions result in an ordered neutral lipid core. FS increased the lipid phase polarity of both LV and LP forms. The rotation of these probes in LP was not affected, suggesting a dependence of FS action on lipid-protein interactions. DPH-PA steady-state anisotropy showed that, unlike the LVe form, the LVI form was sensitive to extremely low FS concentrations. The ability of both LV to transfer palmitic acid to albumin was increased, but in a dissimilar manner, by the presence of FS. Such differences in the sensitivity of the LV at different steps of embryogenesis to FS influence the toxic action of this insecticide., Instituto de Investigaciones Bioquímicas de La Plata

A monoclonal antibody (Mab) developed against a partially purified bursal protein extract was found to bind specifically to a single cell type in the cortico-medullary border region of the chicken bursa of Fabricius. These cells were microscopically similar to the bursal secretory dendritic-like cells. A product with an apparent molecular weight of approximately 56 kDa on SDS-polyacrylamide gel electrophoresis was immunopurified from bursal extracts by utilizing this Mab. This product was subjected to peptide digestion and protein sequencing. The two resulting sequences perfectly matched the known sequence of chicken ovoinhibitor. Gene-specific polymerase chain reaction (PCR) primers were designed for the ovoinhibitor, RNA was purified from chicken bursae, and reverse transcription/PCR was performed. Two amplicons with the expected size for ovoinhibitor mRNA were obtained. These data suggest that the gene for ovoinhibitor is expressed in the bursa of Fabricius, and that the bursal secretory dendritic-like cells may be a previously unreported source of ovoinhibitor.

Vitellogenin (VTG) has been widely used as a biomarker of estrogenic exposure in fish, leading to the development of standardized assays for VTG quantification. However, standardized quantitative assays for invertebrate, particularly crustacean, lipovitellin (also known as vitellin [VTN]) are lacking. In this study, a fluorescence-based VTN enzyme-linked immunosorbent assay (ELISA) was developed to quantify microquantities of VTN in the estuarine, sediment-dwelling copepod Amphiascus tenuiremis. This ELISA utilizes a VTN-specific polyclonal antibody developed against amphipod (Leptocheirus plumulosus) embryo VTN and exhibits specificity toward female copepod proteins. In routine assays, the working range of the ELISA was 31.25 to 1,000 ng/ml (75-25% specific binding/maximum antibody binding [B/B0]) with a 50% B/B0 intra- and interassay variation of 3.9% (n = 9) and 12.5% (n = 26), respectively. This ELISA is capable of detecting VTN as low as 2 ng/ml, and can accurately detect VTN in as few as four copepods. The ELISA significantly discriminated positive (gravid female) and negative (male) samples, and was suitable for screening endocrine toxicity in copepods. Stage-I juvenile copepods were individually reared to adults in aqueous microvolumes of the phenylpyrazole insecticide, fipronil, and whole-body homogenate extracts were assayed for VTN levels. Fipronil-exposed virgin adult females, but not males, exhibited significantly higher levels of VTN relative to control males and females. This crustacean VTN ELISA is likely useful for evaluating endocrine activity of environmental toxicants in copepods and other crustacean species.

Ovoinhibitor is a serine protease-inhibiting protein that was originally purified from egg whites. It is secreted by the oviduct under the control of estrogen and progesterone and it specifically inhibits serine proteinases such as trypsin and chymotrypsin. During recent attempts to raise monoclonal antibodies (Mabs) against chicken bursa of Fabricius proteins, one Mab was produced that specifically recognized chicken ovoinhibitor. This was the first demonstration of ovoinhibitor in an avian immune organ. We presently report on the expression of an ovoinhibitor-like molecule by the pituitary of the chicken as revealed by immunocytochemistry and RT-PCR. Immunofluorescent dual staining experiments using the mouse anti-ovoinhibitor Mab in conjunction with polyclonal antibodies against various hypophysial hormones revealed partial co-localization of an ovoinhibitor-like molecule with growth hormone (GH), luteinizing hormone (LH), and pro-opiomelanocortin (POMC), in a subset of the respective hormone producing cells. By contrast, no co-localization with prolactin (PRL) could be reliably demonstrated. RT-PCR of hypophysial mRNA using ovoinhibitor gene-specific primers yielded an amplicon that was 20% shorter than predicted on the basis of the published ovoinhibitor sequence. Sequencing revealed that of the represented exons only the central portion was expressed in the pituitary and that both 5′ and 3′ ends of each exon had been truncated. While expression of ovalbumin-like serine protease inhibitors (serpins) has been previously reported in the rat pituitary, to our knowledge, this is the first report of a Kazal-type serine protease inhibitor in the vertebrate neuroendocrine system.

Chicken ovoinhibitor cDNA was prepared by reverse transcriptase-polymerase chain reaction (RT-PCR) using chicken oviduct mRNA. The ovoinhibitor cDNA was successfully cloned downstream from the AOXI promoter of pPICZalphaA plasmid vector to facilitate its expression in the methylotrophic yeast Pichia pastoris. The pPICZalphaA carrying the ovoinhibitor cDNA was integrated into the Pichia genome. The secreted recombinant ovoinhibitor was purified by ion-exchange chromatography on a DEAE sepharose column. The recombinant ovoinhibitor had a molecular mass of 49 kDa, as determined from sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and time of flight-mass spectrometry (TOF-MS) analyses. The recombinant ovoinhibitor, just as the native ovoinhibitor, showed inhibitory activity against trypsin, chymotrypsin and elastase.

A total of 272 Cotswold pigs (17 +/- 1 d) were utilized in three experiments to evaluate the nutritive value of spray-dried egg proteins for early-weaned pigs. In all experiments, pigs were stratified by sex and initial BW and then assigned randomly to experimental diets. In Exp. 1, four corn-soybean meal-based diets containing 7% of either spray-dried porcine plasma (SDPP), spray-dried technical albumen (SDTA), SDTA stored at 70 degrees C for 3 d (SDTA-ht), or spray-dried whole egg (SDWE) were assigned to five pens each with four pigs for a 3-wk study period. Average daily gain, ADFI, and gain:feed ratio (G:F) were determined. At the end of wk 3, five pigs per treatment were killed to determine ileal AA and energy digestibilities, as well as Enterobacteriaceae counts. Compared with the SDPP diet, ADG and G:F were lower (P0.05) for SDTA-, SDTA-ht- and SDWE-containing diets. Apparent ileal digestibilities of cystine, histidine, isoleucine, methionine, and threonine in the SDPP diet were lower (P0.05) than in diets containing spray-dried egg products. Ileal digestible energy content did not differ (P0.05) in all diets (3.1 to 3.2 Mcal/kg). Enterobacteriaceae counts were lower in the SDTA-ht diet than in either the SDTA or SDWE diets (P0.05). In Exp. 2, the effect of substituting SDPP with varying levels of SDTA was investigated. Diets were randomly assigned to five pens (except for the 100% SDTA diet, which had four pens), each with four pigs. Average daily gain, ADFI, and G:F decreased linearly as the level of SDTA was increased in the diet (P0.05). Replacing SDPP with SDTA at 25 or 50% had no effect on pig performance (P0.10). In Exp. 3, phase I diets containing 0, 25, or 50% SDTA in place of SDPP (7% of the diet) were each assigned at random to eight pens each with four pigs for a 14-d period, after which all pigs were switched to a common phase II diet lacking both SDPP and SDTA for another 14 d. Average daily feed intake and ADG did not differ among all diets in phase I and II and overall (d 0 to 28). Pigs fed the diet containing 50% SDTA in phase I had lower (P0.05) G:F than those fed the SDPP diet. The results indicate that technical albumen can replace 25 to 50% of SDPP in early-weaned pig diets without compromising performance, and further suggest that heat-treated SDTA may affect intestinal microbial population in pigs.

The use of alternative proteins in milk replacer has been evaluated for their ability to decrease the cost of milk replacers without negatively impacting performance of the calf. Three studies were conducted to evaluate the performance of calves fed milk replacer utilizing liquid egg as an alternative protein and to determine the optimal concentration of liquid egg to include in milk replacers. Calves in trials 1 and 2 were assigned to a control diet of all milk protein replacer (MILK) or a diet formulated to contain 5% of the diet (13.5% of the protein) from liquid egg (5% EGG). Calves in trial 3 were assigned to one of four diets: the control (MILK) and 5% EGG diets fed in trials 1 and 2, or diets formulated to contain either 10 or 15% of the diet (27 or 40.5% of the protein) from liquid egg (10% EGG, 15% EGG). For all experiments, milk replacers were formulated to contain 20% protein, 20% fat and were fed at 454 g/d reconstituted to 12% DM. Production of the diets containing egg protein utilized breaker eggs that were pasteurized during manufacturing. Holstein bull calves (n = 44 for experiment 1, n = 38 for experiment 2, and n = 120 for experiment 3), were purchased from an area sale barn. Calves were housed in individual hutches with water available free choice starting on d 0. A commercially available calf starter was offered free choice beginning on d 7 for experiments 1 and 2 and on d 1 for experiment 3. Feed intake, scour scores, and antibiotic treatments were recorded daily. For experiment 1, calves fed 5% EGG had greater weight gains than calves fed MILK. No differences in average daily feed intake were observed. For experiment 2, weight gains tended to be lower with 5% EGG, whereas feed intakes and gain to feed ratios were similar between calves fed MILK or 5% EGG. For experiment 3, as the amount of egg in the diet increased, weight gain decreased in a linear fashion during the milk replacer feeding period, but the decrease in gain was significant only with the 15% EGG diet. These results indicate that egg is an effective alternative protein source to milk protein in calf milk replacers when fed at levels up to 10% of the diet in a conventional feeding program of 0.45 kg per head per day.

In this article, the influence of factors related to different levels (seg, provincial, county and household) on the proportion of protein intake from animal food was evaluated by using multi-level modeling. It was found that after being adjusted by individual factors, the factors related to the household, such as household income, dietary habit and knowledge of nutrition were the most important factors affecting the individual's showed animal protein intake. In addition, the results showed that the difference of animal protein intake in various places depended not only on the increase of household income, but also dietary behavior and agriculture crops in different areas. Comparison of different models indicates that in analyzing the data from large-scale health survey with hierchical structure, multi-level modeling is strongly recommended.

Vitellogenesis is the process of accumulation of vitellogenin (Vg) in rapidly growing oocytes of oviparous animals and its' subsequent transformation into lipovitellin (Lv). Lipovitellin, which forms the major yolk protein, serves as a principal nutrient reserve for the developing embryo. In the present study, Vg and Lv were purified from the hemolymph and ovary, respectively of the crab Scylla serrata by gel filtration followed by preparative gel electrophoresis. It was observed that purified Vg, but not Lv, possessed an intrinsic protease activity with which it underwent autoproteolysis giving rise to several smaller proteins. Furthermore, urea-mediated unfolding studies by UV-spectral analysis revealed clearly that Vg was easily disrupted by urea whereas Lv was resistant. Taken together, these results suggest that although Lv had a stable conformation, its precursor Vg was labile and highly sensitive to degradation. Another aspect that was investigated in the present study was the immunological kinship of crab Vg and Lv to mammalian atherogenic lipoproteins, the low density lipoprotein (LDL), very low density lipoprotein (VLDL), and apolipoprotein B (apoB). By Western blot analysis, it was demonstrated that crab Vg and Lv were immunoreactive to antibodies to human LDL, VLDL, and apoB. These observations suggest the existence of common epitope recognition sites in crab Vg and mammalian lipid transferring proteins. This corroborates well with our earlier study on the recognition of crab Vg receptor by mammalian lipoproteins.

Changes in water and ion binding that occur during egg protein denaturation can be detected by measuring the dielectric properties. The dielectric properties of egg yolk, egg white and egg ovalbumin were tested from 25 to 105 degrees C at 11 frequencies from 300-2450 MHz. DSC was used to determine the temperature of protein denaturation. Both the dielectric constant and loss factor of egg yolk decreased due to denaturation of the protein lipovitellin. The dielectric constant increased at the initial denaturation and decreased after the complete denaturation and aggregation of egg ovalbumin in both egg white and ovalbumin.

Egg skin prick test (SPT) and/or radioallergosorbent test (RAST) positivity has been described in infants and children with a food allergy, or in infants at high risk of atopy who have never eaten eggs. Clinical reactions are also observed when some of these children or infants eat eggs for the first time.A prospective study was made of 107 atopic dermatitis (AD) children (66 boys, 41 girls) aged 1-19 months (median 5 months) who had never ingested egg, to compare the outcome of a first oral egg challenge and the results of albumen and yolk SPTs and RASTs.The egg challenge (conducted at age 12-24 months: mean 16 months, median 15 months) was positive in 72/107 children (67.3%). The reactions were immediate or early (first 6 h) in 56/72 (77.8%). The most severe (all within the first 6 h) were one case of anaphylactic shock (1.4%), three cases of laryngeal oedema (4.1%) and one serious attack of asthma (1.4%). The skin weal diameter at and above which reactions always occurred was 5 mm for both albumen and yolk. They were, however, also observed in the complete absence of a weal. The outcome of the challenge was always positive when the specific IgEs (sIgE) for albumen and yolk were99 KU/L andor = 17.5 KU/L, respectively. Here, too, reactions were noted even when sIgE levels were0.35 KU/L.AD children who have never eaten eggs may be sensitized and display reactions at the first ingestion. The percentage of reactions in this series was by no means negligible. These findings were observed in children with mild as well as moderate-severe AD when first examined. SPT for albumen and yolk diameteror = 5 mm, and sIgE for albumen99 KU/L and for yolkor = 17.5 KU/L were 100% specific in predicting the outcome of the challenge. It may thus be concluded that children with AD whose SPT and/or RAST for albumen and/or yolk are equal to or higher than these cut-off values should not be subjected to the oral challenge when consideration is given to the introduction of egg in their diet. Even when these cut-offs are not reached, however, clinical reactions to the challenge cannot be ruled out a priori, and it should be preferably performed in a protected environment, such as a hospital.

We have examined 370 infants less than 12 months of age with atopic dermatitis about food allergies, especially by egg white antigens. Since the results of the skin scratch test and serum specific IgE antibody test often correspond to each other, only the serum specific IgE antibody test was given to infants over 6 months of age. An oral provocation test using boiled egg white was given to 176 patients, and 52 of them showed immediate positive reaction. The number of patients with a positive reaction was much fewer than expected. This may be due to lowered levels of egg white antigens from being boiled, and the majority of patients that took the test were over 12 months of age. Those infants with atopic dermatitis often react positively to both serum specific IgE antibody tests and skin scratch tests, therefore follow up studies on changes in the level of serum IgE antibody and reaction to oral provocation tests with infants over 6 or 7 months of age must be done to determine if egg whites need to be eliminated from their diet or not.

Chicken eggs are used extensively as an excellent source of dietary proteins. These proteins have many functional properties, making them valuable food ingredients. However, eggs are a frequent cause of food hypersensitivity, especially in children. Of major concern to food processors is the inadvertent cross-contact of food products with allergenic residues, which could result in potentially life-threatening reactions in those with a food allergy. The aim of the present study was to develop an enzyme-linked immunosorbent assay (ELISA) for the detection of undeclared egg residues in foods. Commercially purified ovalbumin (OVA) and dehydrated egg white solids were used as antigens to induce antibodies in rabbits and goats. Reference pasta standards and various food samples were extracted, then clarified by centrifugation. Goat anti-egg white antibodies were used as the capture reagent, nonspecific sites were blocked with gelatin, then standard and sample extracts were added. Rabbit anti-OVA antibodies were used as detector antibodies, followed by addition of commercial goat anti-rabbit IgG antibody labeled with alkaline phosphatase and subsequent substrate addition. Twenty brands of egg-free pasta (two lots each) were analyzed using the ELISA. Fourteen common pasta ingredients were also evaluated for cross-reactivity problems in the method. The detection limit of the assay was 1 ppm spray-dried whole egg. Fifty-five percent (22 samples) of the egg-free pasta samples tested positive for the presence of undeclared egg residues, with values ranging from 1 to >100,000 ppm. Minimal cross-reactivity was encountered in general, but portobello mushrooms and basil caused some minor matrix effects. This sandwich-type ELISA method can be used to detect undeclared egg residues in processed foods and to evaluate industrial clean-up operations.

For centuries, the edible nests of Collocalia spp. ("Bird's Nests") have been used as a Chinese delicacy that had been claimed to be an effective health-giving tonic. However, clinical studies indicated that in Singapore, Bird's Nest is the most common cause of food-induced anaphylaxis in children, which could lead to potentially life-threatening allergenic reactions. The purpose of this study was to characterize the major allergens in Bird's Nest by using the combined technologies of two-dimensional gel electrophoresis (2-DE), immunochemistry, N-terminal protein sequencing, and mass spectrometry. Results from the immunostaining of the Western blots of the Bird's Nest 2-DE separated proteins with the sera from allergic patients indicated the presence of a major allergen of 66 kDa. Initial searches of the matrix assisted laser desorption/ionization--time of flight--mass spectrometry (MALDI-TOF-MS) tryptic peptide masses of the allergen in the SWISS-PROT and NCBI nonredundant databases revealed that this protein was novel. Based on the partial protein sequence information obtained from N-terminal microsequencing and nanoelectrospray-tandem MS, the 66 kDa immunoreactive allergen was found to be homologous to ovoinhibitor, a Kazal-type serine protease inhibitor, which is one of the dominant allergens found in chicken egg white.

A highly sensitive and specific chemiluminescent immunoassay (CLIA) was developed for quantification of vitellogenin (Vg) in five salmonids. The CLIA for salmon Vg was performed using the two-site method, with anti-masu salmon β′-component as primary antibody and chemiluminescent acridinium-labeled anti-rainbow trout lipovitellin F(ab)′ 2 as the second antibody. Using cutthroat trout Vg as the standard, the working range of the CLIA was from 60 pg to 500 ng Vg/ml. Intra- and inter-assay coefficients of variation ranged from 3.04 to 6.67% and 3.23 to 5.86%, respectively. For the various salmonid species, serially diluted samples of serum from vitellogenic fish ran parallel to their purified Vg standard curve in the CLIA. In male cutthroat trout maturing during the 4 months before spawning, serum Vg levels ranged from 1.56 to 8000 ng/ml. High levels of Vg in some individuals may have resulted from temporary elevation of estradiol-17β levels in the same fish during December or January (1–2 months before spawning). This is the first report on changes in serum Vg levels in maturing male trout using CLIA, the most sensitive assay for Vg yet developed.

Identification of targets of estrogen is an important step in understanding the mechanisms of estrogen action. A two-step strategy was developed to identify estrogen-responsive genes (ERGs) in chick liver. Initially, differential-display, reverse transcription polymerase chain reaction (DDRT-PCR) was introduced to isolate ERGs. Isolated ERGs were then analyzed using Northern blot hybridization. A number of differentially expressed cDNA fragments were isolated following estrogen exposure. Four cDNA fragments that displayed dramatic change after estrogen administration were identified as liver adenylosuccinate lyase (ADL), phenobarbital-inducible cytochrome P-450 (CYP450), ovoinhibitor, and glutathione-dependent prostaglandin D2 synthase (PGDS). Time sequence analysis showed that estrogen-induced alteration occurred as early as 0.5 h and peaked between 1 and 4 h after estrogen exposure. Nuclear runoff assay indicated that estrogen significantly increased the transcription rate of these genes. To determine whether the observed alteration was due to the direct effect of estrogen, protein synthesis was inhibited by cycloheximide (CHX) during stimulation by estradiol, Estrogen-mediated upregulation of PGDS was completely abolished by a concurrent treatment with CHX, suggesting that its activation requires the participation of some newly synthesized factor(s). In contrast, CHX did not affect the expression of other genes, indicating the alteration is a direct response to estrogen. In conclusion, ADL, CYP450, ovoinhibitor, and PGDS represent the novel targets of estrogen, which regulates the transcriptional activity of these genes.

Proteinaceous materials in the air can be highly allergenic and result in a range of immunologically mediated respiratory effects, including asthma. We report on the largest evaluation of exposure to date of airborne egg protein concentrations in an egg breaking and processing plant that had cases of occupational asthma. Personal air samples for egg protein were analyzed in duplicate on each PTFE filter using two analytical methods: (1) a commercial assay for non-specific total protein, and (2) indirect competitive inhibition assay using an ELISA method to quantify specific egg protein components. The highest concentrations were found in the egg washing room (mean exposure 644 microg/m3) and breaking room (255 microg/m3), which were also the areas where the risk of being sensitized was the greatest. There was excellent quantitative agreement between the airborne concentrations of total protein and sum of the specific protein antigens (ovalbumin, ovomucoid, and lysozyme). The correlation coefficient of the log-transformed data from the two methods was 0.88 (p < 0.0001). Size-selective sampling also indicated that most of the aerosol was capable of reaching the small airways. The methods described can be utilized to evaluate employee exposure to egg proteins. Exposure documentation, coupled with recommended exposure reduction strategies, could facilitate prevention of future employee sensitization and allergic respiratory responses by identifying high-exposure jobs and evaluating control measures.

Lipovitellin II (Lv II), the major yolk protein of the anomuran crab Emerita asiatica, was purified using heparin-sepharose affinity column chromatography. The purified Lv II was a glycoprotein as it was stainable with periodic acid-Schiff's reagent. Quantitative analysis of sugars showed the presence of fucose, mannose, galactosamine, N-linked oligosaccharides, as well as O-linked oligosaccharides containing N-acetyl hexosamine as the terminal residue. The amount of N-linked oligosaccharides is higher than that of the O-linked oligosaccharides. Biogel P-4 column chromatographic separation of the radiolabeled oligosaccharides of Lv II showed the presence of five different O-linked oligosaccharides and four different N-linked oligosaccharide species. HPTLC separation of the neoglycolipids prepared from the O-linked oligosaccharides also showed the presence of five different O-linked oligosaccharide species. N-linked oligosaccharides contain significant quantities of mannose. Unisil column chromatographic purification in conjunction with HPTLC separation revealed three neutral glycolipid species such as monoglycosylceramide, diglycosylceramide, and triglycosylceramide in the Lv II. The functional significance of these carbohydrate components of the major yolk protein during embryogenesis of the sand crab is discussed.

The yolk protein, lipovitellin (Lv) was purified from ovaries of mature female zebrafish (Danio rerio) by gel filtration and anion exchange chromatography. Polyclonal antibodies against Lv were raised in rabbits. Anti-Lv IgG was purified by affinity chromatography. SDS-PAGE followed by Western blotting was performed to analyse the specificity of the antibody and the immunological similarities between Lv and vitellogenin (Vtg). Anti-Lv IgG was used to develop a direct non-competitive sandwich ELISA to measure Vtg concentrations of whole body homogenate (WBH) in zebrafish. The intra- and interassay variabilities were 5.8% and 10.4%, respectively. The sensitivity was 0.2 ng Vtg x ml(-1) and the practical detection limit was 40 ng Vtg x g(-1) fish (wet weight). Adult male zebrafish were exposed to a nominal water concentration of 10 ng x l(-1) of ethinylestradiol (EE2) in a semi-static exposure system for 7 days. Compared with the control group, exposure to 10 ng EE2 x l(-1) induced a 200-fold increase in Vtg levels.

Chicken alpha- and beta-lipovitellin are derived from parent vitellogenin proteins and contain four subunits (125, 80, 40, and 30 kDa) and two subunits (125 and 30 kDa), respectively. Metal analyses demonstrate both are zinc proteins containing 2.1 +/- 0.2 mol of zinc/275 kDa per alpha-lipovitellin and 1.4 +/- 0.2 mol of zinc/155 kDa per beta-lipovitellin, respectively. The subunits of beta-lipovitellin, Lv 1 (MW 125 kDa) and Lv 2 (MW 30 kDa), are separated by gel exclusion chromatography in the presence of zwittergent 3-16. Zinc elutes with Lv 1, suggesting that this subunit binds zinc in the absence of Lv 2. The subunits of alpha- and beta-lipovitellin were separated by SDS-PAGE, digested with trypsin, and mapped by reverse-phase HPLC. The peptide maps of the 125-kDa subunits from alpha- and beta-lipovitellin are essentially identical. Similar results are obtained for the 30-kDa subunits of both lipovitellins. The sequences of five and four peptides of the 125-kDa subunit of alpha- and beta-Lv, respectively, and two peptides of the 30-kDa subunit of alpha- and beta-lipovitellin were determined and match those predicted from the gene for vitellogenin II, Vtg II. Comparison of the amino acid composition of the 125- and 30-kDa subunits of alpha- and beta-lipovitellin support the conclusion that they originate from the same gene. The sequences of peptides from the 80- and 40-kDa subunits of alpha-lipovitellin have not been found in the NCBI nonredundant data bank. The 27-amino acid N-terminal sequence of the 40-kDa protein is 56% similar to the last third of the Lv 1-coding region of the Vtg II gene, suggesting it may come from an analogous region of the Vtg I gene. We propose a scheme for the precursor-product relationship of Vtg I.

Ecological niches of Staphylococcus aureus are the anterior nares. Carriage of Staphylococcus aureus in the nose appears to play a key role in the epidemiology and pathogenesis of infection. Numerous studier have shown that elimination of nasal carriage using Mupirocin also eliminated hand carriage and the spread of infections in hospitals. Lipovitellin-Salt-Mannitol Agar was used for screening, isolation and presumptive identification of Staphylococcus aureus from nasal carriers. From November; 97 to August'98, 724 nasal swabs were cultured and 18.23% of health care workers were found to be nasal carriers of Staphylococcus aureus. Of these 12.15% were carriers of MRSA. The carrier rate was highest in December' 97 (32.07%). All MRSA carriers were treated with local application of Mupirocin for three days. A study of the antibiogram of the clinical isolates during the corresponding period showed 100% susceptibility of MRSA to Vancomycin. Susceptibility of MRSA to Clindamycin, Netilmycin, RifampicinOfloxacin was 86.6%, 69.5%, 66%64.7% respectively.

For years, eggs have been held up as a powerhouse of nutrition. This reputation has been due to eggs’ exceptional nutrition profile as a nutrient-dense food containing high quality protein and a substantial amount of many essential vitamins and minerals. Unfortunately their position on the nutrition pedestal fell with the discovery that they are also a source of dietary cholesterol. The most recent scientific research not only returns eggs to their golden past, but elevates their position as a functional food and ultimately provides more reasons than ever to consume eggs. In February 2000, scientists convened at a conference in Amelia Island, Florida, to discuss the latest research about the role of eggs in disease prevention and the promotion of health. This supplement of the Journal of the American College of Nutrition (JACN)presents compelling scientific evidence about eggs’ functional food attributes, reaffirms that eggs have a minimal effect on blood cholesterol levels and presents new research on the contribution of eggs to the American diet. For health professionals, this issue provides a new scientifically based viewpoint on eggs and their role in health and nutrition, a viewpoint that should be imparted to all consumers in an effort to ensure optimal health and well-being.

There has been debate among athletes and nutritionists regarding dietary protein needs for centuries. Although contrary to traditional belief, recent scientific information collected on physically active individuals tends to indicate that regular exercise increases daily protein requirements; however, the precise details remain to be worked out. Based on laboratory measures, daily protein requirements are increased by perhaps as much as 100% vs. recommendations for sedentary individuals (1.6-1.8 vs. 0.8 g/kg). Yet even these intakes are much less than those reported by most athletes. This may mean that actual requirements are below what is needed to optimize athletic performance, and so the debate continues. Numerous interacting factors including energy intake, carbohydrate availability, exercise intensity, duration and type, dietary protein quality, training history, gender, age, timing of nutrient intake and the like make this topic extremely complex. Many questions remain to be resolved. At the present time, substantial data indicate that the current recommended protein intake should be adjusted upward for those who are physically active, especially in populations whose needs are elevated for other reasons, e.g., growing individuals, dieters, vegetarians, individuals with muscle disease-induced weakness and the elderly. For these latter groups, specific supplementation may be appropriate, but for most North Americans who consume a varied diet, including complete protein foods (meat, eggs, fish and dairy products), and sufficient energy the increased protein needs induced by a regular exercise program can be met in one's diet.

The microsomal triglyceride transfer protein (MTP) and apolipoprotein B (apoB) belong to the vitellogenin (VTG) family of lipid transfer proteins. MTP is essential for the intracellular assembly and secretion of apoB-containing lipoproteins, the key intravascular lipid transport proteins in vertebrates. We report the predicted three-dimensional structure of the C-terminal lipid binding cavity of MTP, modeled on the crystal structure of the lamprey VTG gene product, lipovitellin. The cavity in MTP resembles those found in the intracellular lipid-binding proteins and bactericidal/permeability-increasing protein. Two conserved helices, designated A and B, at the entrance to the MTP cavity mediate lipid acquisition and binding. Helix A (amino acids 725–736) interacts with membranes in a manner similar to viral fusion peptides. Mutation of helix A blocks the interaction of MTP with phospholipid vesicles containing triglyceride and impairs triglyceride binding. Mutations of helix B (amino acids 781–786) and of N780Y, which causes abetalipoproteinemia, have no impact on the interaction of MTP with phospholipid vesicles but impair triglyceride binding. We propose that insertion of helix A into lipid membranes is necessary for the acquisition of neutral lipids and that helix B is required for their transfer to the lipid binding cavity of MTP.

Knowledge about cross reactivities among food proteins of plant or animal origin is getting more and more important. Cross reaction provoking often clinical symptoms may be based on close taxonomical relations or on the presence of "archaic", ubiquiter protein structures preserved during phylogenesis. The most significant cross reactivities characterized by increasing incidence are between pollens and foods of plant origin and between latex and fruits.

Background: Eggs are among the foods most frequently causing allergy. Hen eggs are the most important. Those of other birds are of lesser significance. Objective: We report an unusual case of food allergy after consumption of eggs from duck and goose in an adult patient without hen egg allergy. Methods: Skin prick tests were performed with fresh white and yolk from eggs of duck and goose and egg white, egg yolk, ovalbumin, and ovomucoid from hen egg. Specific serum IgE was measured to hen egg proteins. SDS-PAGE and IgE immunoblotting were carried out with egg white extracts from hen, duck, and goose. Results: Skin tests were positive to egg whites from duck and goose. The skin tests and specific serum IgE were negative to hen egg proteins. Immunoblotting demonstrated the presence of specific IgE to a proteic band of molecular weight around 45 kd. Conclusions: We report a patient with an IgE-mediated allergy to egg white from duck and goose without hen egg allergy. Ovalbumin seems to be the responsible protein. The antigenic determinant of this protein seems to be specific of order Anseriforme and it is not present in the ovalbumin of order Galliforme. (J Allergy Clin Immunol 2000;105:834-6.)

On the basis of the rate of animal growth, proteins have been traditionally classed as high quality, such as egg and milk protein, or low quality such as gluten. In general, vegetable proteins are of low quality but soy protein is an exception. The paper by Capristo et al. in this issue of the journal has shown that enteral formulations consisting of soy protein are as effective nutritionally as enteral formulations containing milk protein.

The developmental fate of the vitellogenin-derived yolk protein, lipovitellin (Lv), was investigated in winter flounder embryos and yolk-sac larvae. Since Lv is present as only one major polypeptide in ovulated winter flounder eggs, unlike the multiple yolk polypeptides found in the mature eggs of most teleosts, this system is presented as a simpler model of yolk protein structure and utilization during teleostean development. Winter flounder Lv is cleaved during embryogenesis from a 94 kD polypeptide at fertilization to 67 kD and 26 kD polypeptides at hatching. The rate of this proteolytic processing is slow during early embryonic development, but enters a more rapid phase between days 8 and 12 post-fertilization in embryos reared at 4-5 degrees C, and approaches 50% completion at day 10. Lv processing is essentially complete 3 days before hatching; nevertheless, major degradation of the Lv peptide by the developing winter flounder does not occur until after hatching. The Stokes radius of Lv changes only moderately following processing, from 4.50 nm in unfertilized eggs to 4.19 nm in late embryos and newly hatched larvae, whereas the processed Lv retains its heat stability relative to other yolk polypeptides. Nearly 50% of its lipid content, however, is released from the Lv particle during embryogenesis, concomitant with cleavage of the Lv 94 kD polypeptide. Lv processing may thus render a portion of the yolk protein-associated lipid more accessible to the developing embryo, whereas other yolk components are retained for later use by the winter flounder larva. Alternately, removal of lipid may lead to proteolytic vulnerability of the Lv polypeptide. In either case, only a portion of the lipid moiety of the Lv particle appears to play a significant nutritive role for the embryo, whereas its protein component is reserved for larval use. J. Exp. Zool. 284:686-695, 1999.

Two forms of vitellogenin (Vg), Vg A and Vg B, were identified in serum from estrogen-treated barfin flounder (Verasper moseri). Structural changes of lipovitellins (Lvs) derived from the two Vgs were examined during vitellogenesis and oocyte maturation. Two Lvs, vLv A and vLv B, were identified electrophoretically and immunologically in postvitellogenic oocytes. Each appeared to be composed of distinct heavy chains (vLvH A, M(r) 107,000, and vLvH B, M(r) 94,000) and light chains (vLvL A, M(r) 30,000, and vLvL B, M(r) 28,000) when analyzed by SDS-PAGE. Results from N-terminal amino acid sequencing and Western blotting using antisera to vLvH A and vLvH B verified that there are two Vg polypeptides in serum from estrogen-treated fish, Vg A (M(r) 168,000) and Vg B (M(r) 175,000), which give rise to vLvH A-vLvL A and vLvH B-vLvL B, respectively. N-terminal sequencing revealed two sequences for both phosvitin and beta'-component, supporting the concept of duality for all three classes of Vg-derived yolk proteins. During oocyte maturation, native dimeric vLv B was dissociated into a native M(r) 170,000 monomer (oLv B). Meanwhile, vLv A was extensively cleaved including complete degradation of vLvH A into free amino acids. We propose that the quantitative ratio of vLv A to vLv B in postvitellogenic oocytes regulates the buoyancy of the spawned pelagic eggs by controlling availability of free amino acids which function as osmotic effectors during oocyte hydration. The vLv A/vLv B ratio likely also controls the proportional availability of different types of nutrients, free amino acids versus Lv, for use during embryonic development.

The process of assembly of apolipoprotein (apo) B-containing lipoprotein particles occurs co-translationally after disulfide-dependent folding of the N-terminal domain of apoB but the mechanism is not understood. During a recent database search for protein sequences that contained similar amphipathic beta strands to apoB-100, four vitellogenins, the precursor form of lipovitellin, an egg yolk lipoprotein, from chicken, frog, lamprey, and C. elegans appeared on the list of candidate proteins. The X-ray crystal structure of lamprey lipovitellin is known to contain a "lipid pocket" lined by antiparallel amphipathic beta sheets. Here we report that the first 1000 residues of human apoB-100 (the alpha(1) domain plus the first 200 residues of the beta(1) domain) have sequence and amphipathic motif homologies to the lipid-binding pocket of lamprey lipovitellin. We also show that most of the alpha(1) domain of human apoB-100 has sequence and amphipathic motif homologies to human microsomal triglyceride transfer protein (MTP), a protein required for assembly of apoB-containing lipoproteins. Based upon these results, we suggest that an LV-like "proteolipid" intermediate containing a "lipid pocket" is formed by the N-terminal portion of apoB alone or, more likely, as a complex with MTP. This intermediate produces a lipid nidus required for assembly of apoB-containing lipoprotein particles; pocket expansion through the addition of amphipathic beta strands from the beta(1) domain of apoB results in the formation of a progressively larger high density lipoprotein (HDL)-like, then very low density lipoprotein (VLDL)-like, spheroidal lipoprotein particle.

The assembly of atherogenic lipoproteins requires the formation in the endoplasmic reticulum of a complex between apolipoprotein (apo)B, a microsomal triglyceride transfer protein (MTP) and protein disulphide isomerase (PDI). Here we show by molecular modelling and mutagenesis that the globular amino-terminal regions of apoB and MTP are closely related in structure to the ancient egg yolk storage protein, vitellogenin (VTG). In the MTP complex, conserved structural motifs that form the reciprocal homodimerization interfaces in VTG are re-utilized by MTP to form a stable heterodimer with PDI, which anchors MTP at the site of apoB translocation, and to associate with apoB and initiate lipid transfer. The structural and functional evolution of the VTGs provides a unifying scheme for the invertebrate origins of the major vertebrate lipid transport system.

The effects of dietary egg on the age-related progression of impaired glu- cose tolerance and glomerulonephropathy in diabetes-prone BHWCdb rats were stud- ied. This rat strain mimics the human with NIDDM. The development of impaired glucose tolerance was delayed in rats fed the whole-egg diet, however, feeding this diet resulted in elevated hepatic weight but had no effect on the age-related changes in renal lesions or renal function. We conclude that in this animal model for NIDDM, the development of glomerulonephropathy is independent of the development of im- paired glucose tolerance and that diet can affect the time course for impaired glucose tolerance without affecting renal disease development. (P.S.E.B.M. 1998, Vol 2191

A new algorithm for analysis of the homology and genetic semihomology in protein sequence is described. It assumes the close relation between the compared amino acids and their codons in related proteins. The algorithm is based on the network of the genetic relationship between amino acids and, thus differs from the commonly used statistical matrices. The results obtained by using this method are more comprehensive than used at present, and reflect the actual mechanism of protein differentiation and evolution. They concern: (1) location of homologous and semihomologous sites in compared proteins; (2) precise estimation of insertion/deletion gaps in non-homologous fragments; (3) analysis of internal homology and semihomology; (4) precise location of domains in multidomain proteins; (5) estimation of genetic code of non-homologous fragments; (6) construction of genetic probes; (7) studies on differentiation processes among related proteins; (8) estimation of the degree of relationship among related proteins; (9) studies on the evolution mechanism within homologous protein families and (10) confirmation of actual relationship of sequences showing low degree of homology.

An egg protein, lysozyme, is a still unlabeled additive currently used in cheese preparation. Furthermore, the WHO-FAO committee considers it innocuous. However, 31% of children and 8% of adults with food allergies are allergic to eggs. This work aimed to determine the percentage of patients sensitized to lysozyme from a population of egg-allergic patients. Specific IgE was determined with Cap RAST in 52 patients clinically allergic to egg. Thirty-five percent of egg-allergic patients had antilysozyme IgE. Given this high incidence of lysosozyme sensitization, it seems that the presence of lysozyme should be indicated on food labels.

A dry egg yolk ingredient called Eggcellent has 74% less fat and 90% less cholesterol than liquid egg yolks, when reconstituted on an equal protein basis. The phospholipids and proteins are retained, enabling the ingredient to have the taste and texturizing properties of fresh egg yolk. Using the new yolk, it is possible to significantly improve the acceptability of low-fat, low-cholesterol bakery products, scrambled eggs and mayonnaise dressings without losing nutritional claims. The structures and functional properties of egg yolk components and the conditions required to optimize their benefits in foods are reviewed. The lipoproteins of low-fat, low-cholesterol yolk have valuable properties as flavorants, texturizers, foaming agents, emulsifiers, antioxidants, colorants, and nutraceuticals.

In connection with a study on the prophylaxis of infectious diarrhea with specific egg yolk antibodies, the systemic availability of colostral bovine immunoglobulin G (bIgG) and chicken immunoglobulin Y (IgY) after feeding egg powder was investigated on 26 newborn calves from 23 different farms. Blood was sampled daily and at the same day time from these calves in the first 14 days of life. During the feeding of colostrum, the mean bIgG concentration was highest at day 1 post natum with a value of 9.3 mg/ml serum. Thereafter, the mean bIgG level was reduced continuously to a significant lower concentration of 4.9 mg/ml serum at day 12 post natum and remained nearly constant at 5.2 mg/ml till to the end of the observation period. Total protein concentrations in the serum did not change and plateaued at a mean value of 56.2 mg/ml (SD 11.2). The number of colostrum meals had no significant effect on the mean bIgG concentrations during that period. The individual variation of bIgG concentrations was very high on every day of the sampling period. The mean coefficient of variation was at 52.1 % (SD 5.7). After having described the individual bIgG concentration curves mathematically with a regression curve, two groups with significantly different bIgG elimination constants (k) could be obtained. Thus in one group (n = 10) with k-values of-0.02 a mean half time of serum bIgG of 24.3 days (SD 4.6) was calculated. In the other group of calves (n = 16) with elimination constants of k-0.02, a mean half time of 68.5 days (SD 36.7) could be calculated, possibly because these calves started earlier with their endogenous bIgG production. Additionally, to 18 of these calves 20 g egg powder with an IgY concentration of 15 mg/g was fed up to day 14. Calves had a maximal mean IgY concentration of 1.9 micrograms/ml serum if egg powder feeding started already during the first 12 hours of life. Starting at a later time resulted in a significant reduction of IgY levels. For example, the mean initial IgY concentration dropped to 0.035 micrograms/ml serum after having had the first egg powder application between 25 and 48 hours post natum. Using the individual IgY elimination constant derived from a regression analysis (r2 = 0.84) of the IgY concentration curve, a mean IgY half time of 5.0 days (SD 2.5) could be calculated. To prevent the absorption of heterologous antibodies and consecutively, also to prevent a possible systemic effect, egg powder for prophylactic purposes in newborn calves should be fed after the first 24, better 48 hour, post natum. Most important for the prophylactic effect of specific antibodies on infectious diarrhea is not their systemic but their high local intestinal availability.