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Relationship between biotin-binding proteins from chicken plasma and egg yolk.

ABSTRACT: The plasma of laying hens contains a specific biotin-binding protein that appears to be identical with an egg-yolk biotin-binding protein. Both proteins are saturated with biotin and require elevated temperatures to effect the exchange of [14C]biotin for the protein-bound vitamin. The heat-exchange curve in each case is the same and differs sharply from that of avidin, the egg-white biotin-binding protein. On Sephadex G-100 gel filtration, plasma and yolk biotin-binding proteins were each eluted slightly ahead of avidin (mol.wt. 68,000), suggesting that they are of similar molecular weight. Plasma and yolk biotin-binding proteins required the same ionic strength to be eluted from a phosphocellulose ion-exchange column. Both the plasma and yolk biotin-binding proteins had a pI of 5; avidin has a pI of 10. Plasma biotin-binding protein cross-reacted with antiserum to yolk biotin-binding protein and showed a precipitin line of identity with purified yolk biotin-binding protein. It is suggested that biotin-binding plays an important role in mediating the transport of the vitamin from the bloodstream to the developing oocyte.

SUBMITTER: Mandella RD

PROVIDER: S-EPMC1186112 | biostudies-other | 1978 Nov

REPOSITORIES: biostudies-other

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Biotin-binding protein from chicken egg yolk. Assay and relationship to egg-white avidin.

Project description:1. Biotin in chicken egg yolk is non-covalently bound to a specific protein that comprises 0.03% of the total yolk protein (0.8 mg/yolk). This biotin-binding protein is not detectable by the normal avidin assay owing to the biotin being tightly bound. Exchange of [14C]biotin for bound biotin at 65 degrees C is the basis of an assay for this protein. 2. Biotin-binding protein from egg yolk is distinguishable from egg-white avidin on Sephadex G-100 gel filtration, although the sizes of the two proteins appear quite similar. 3. Biotin-binding protein is denatured at a lower temperature and freely exchanges biotin at lower temperatures than does avidin. 4. The biotin-binding protein in egg yolk is postulated to be responsible for the deposition of biotin in egg yolk. D-[carboxyl-14C]Biotin injected into laying hens rapidly appears in the egg bound to yolk biotin-binding protein and avidin. Over 60% of the radioactivity is eventually deposited in eggs. The kinetics of biotin deposition in the egg suggests a 25 day half-life for an intracellular biotinyl-coenzyme pool in the laying hen.

| S-EPMC1163865 | biostudies-other

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| S-EPMC1136964 | biostudies-other

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| S-EPMC9792406 | biostudies-literature

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| S-EPMC1185825 | biostudies-other

3D Cultures of Salivary Gland Cells in Native or Gelled Egg Yolk Plasma, Combined with Egg White and 3D-Printing of Gelled Egg Yolk Plasma.

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| S-EPMC6861896 | biostudies-literature

Isolation and characterization of cDNA encoding chicken egg yolk aminopeptidase Ey.

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| S-EPMC7172579 | biostudies-literature

Quantitative Lipidome Analysis of Boiled Chicken Egg Yolk under Different Heating Intensities.

Project description:The effects of the four heating intensities (hot-spring egg yolk, HEY; soft-boiled egg yolk, SEY; normal-boiled egg yolk, NEY; and over-boiled egg yolk, OEY) on lipidomes of boiled egg yolks were investigated. The results indicated that four heating intensities had no significant effect on the total abundance of lipids and lipid categories except for bile acids, lysophosphatidylinositol, and lysophosphatidylcholine. However, of all the 767 lipids quantified, the differential abundance of 190 lipids was screened among the egg yolk samples at four heating intensities. Soft-boiling and over-boiling altered the assembly structure of the lipoproteins through thermal denaturation and affected the binding of lipids and apoproteins, resulting in an increase in low-to-medium-abundance triglycerides. The decreased phospholipid and increased lysophospholipid and free fatty acid in HEY and SEY suggests potential hydrolysis of phospholipids under relatively low-intensity heating. Results provide new insights into the effect of heating on the lipid profiles of egg yolk and would support the public's choice of cooking method for egg yolks.

| S-EPMC10301504 | biostudies-literature

Simple and efficient protocol for immunoglobulin Y purification from chicken egg yolk.

Project description:Besides being a common food component broadly consumed worldwide, egg yolk immunoglobulin Y (IgY) has essential therapeutic potentials. In fact, in a time of ever-increasing risk of antibiotic resistance, it is crucial to find new ways to battle infection, and oral administration of preformed specific antibodies represents one of the most attractive approaches against infection. Infectious diseases of bacterial and viral origin in humans and animals can be controlled and passively cured by orally applied IgYs isolated from chicken egg yolks. Despite multiple obvious advantages of oral administration of IgY, harvesting IgY from egg yolk in a pure form is a challenging task. In this study, we developed a fast, simple, cost-effective, and efficient protocol for IgY isolation from chicken egg yolks. First, egg yolk was collected and diluted with 5 volumes of cold distilled water, homogenized, pH adjusted, and centrifuged. Next, the supernatant was collected, to which caprylic acid at concentration of 2% v/v was added, followed by pH adjustment to pH 5.0, centrifugation at 4°C, and collection of the resulting supernatant. This step was repeated twice, with adding 2% v/v of caprylic acid each time. The final supernatant was concentrated using ultrafiltration, and the IgY purity and activities were checked by SDS-PAGE, western blotting, and ELISA. The sequential (2, 2, 2%) addition of caprylic acid yielded IgY with a purity of 63.5, 90.6, and 95.8%, respectively, and reached 97.9% after ultrafiltration at pH 9.0. The IgY activity increased exponentially to reach 99% after the ultrafiltration step. The proposed caprylic-acid-based protocol of IgY purification from the yolk of chicken eggs seems to be simple, fast, direct, and very cheap. This indicates that this protocol has great potential for scale-up processing.

| S-EPMC7936219 | biostudies-literature

Chicken genome analysis reveals novel genes encoding biotin-binding proteins related to avidin family.

Project description:BackgroundA chicken egg contains several biotin-binding proteins (BBPs), whose complete DNA and amino acid sequences are not known. In order to identify and characterise these genes and proteins we studied chicken cDNAs and genes available in the NCBI database and chicken genome database using the reported N-terminal amino acid sequences of chicken egg-yolk BBPs as search strings.ResultsTwo separate hits showing significant homology for these N-terminal sequences were discovered. For one of these hits, the chromosomal location in the immediate proximity of the avidin gene family was found. Both of these hits encode proteins having high sequence similarity with avidin suggesting that chicken BBPs are paralogous to avidin family. In particular, almost all residues corresponding to biotin binding in avidin are conserved in these putative BBP proteins. One of the found DNA sequences, however, seems to encode a carboxy-terminal extension not present in avidin.ConclusionWe describe here the predicted properties of the putative BBP genes and proteins. Our present observations link BBP genes together with avidin gene family and shed more light on the genetic arrangement and variability of this family. In addition, comparative modelling revealed the potential structural elements important for the functional and structural properties of the putative BBP proteins.

| S-EPMC1082904 | biostudies-literature

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