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

1976 ◽  
Vol 157 (2) ◽  
pp. 395-400 ◽  
Author(s):  
H B White ◽  
B A Dennison ◽  
M A Della Fera ◽  
C J Whitney ◽  
J C McGuire ◽  
...  
Keyword(s):  
Binding Protein ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Egg White ◽  
Specific Protein ◽  
Chicken Egg ◽  
Biotin Binding ◽  
Lower Temperature ◽  
Chicken Egg Yolk ◽  
Kinetics Of

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.

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

1978 ◽  
Vol 175 (2) ◽  
pp. 629-633 ◽  
Author(s):  
R D Mandella ◽  
H W Meslar ◽  
H B White
Keyword(s):  
Binding Proteins ◽  
Elevated Temperatures ◽  
Binding Protein ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Egg White ◽  
Similar Molecular Weight ◽  
Precipitin Line ◽  
Ion Exchange Column ◽  
Biotin Binding

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.

scholarly journals Biotin-binding protein from egg yolk. A protein distinct from egg white avidin.

1978 ◽  
Vol 253 (19) ◽  
pp. 6979-6982 ◽  
Author(s):  
H.W. Meslar ◽  
S.A. Camper ◽  
H.B. White
Keyword(s):  
Binding Protein ◽  
Egg Yolk ◽  
Egg White ◽  
Biotin Binding

scholarly journals Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography

2021 ◽  
Vol 13 (2) ◽  
pp. 77-84
Author(s):  
Khoa Nguyen Tran ◽  
Van Song Toan Vo
Keyword(s):  
Recovery Rate ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Phosphorus Recovery ◽  
Purification Process ◽  
Factors Affecting ◽  
Chicken Egg ◽  
Chicken Egg Yolk

Phosvitin from chicken egg yolk, known as a phosphoglycoprotein, owns a very strong metal chelating property due to its polyanionic character. This study aimed to evaluate the factors affecting the purification process and suitable conditions to increase phosvitin’s purity. Phosvitin was separated from yolk granules by using 10% of NaCl solution in 0.05 M NaOH solution and heat treatment which removes lipoprotein from the extracted solution. The highest phosphorus content (58.14 mg) and phosphorus recovery rate (32.4%) were obtained at thermal treatment of 30℃ for 30 minutes. In addition, phosvitin was purified using anion-exchange chromatography (AEC) and gel-filtration chromatography (GFC). The fraction 1 (F1) obtained from AEC using UNO-Sphere Q at pH 8 had the recovery rate of phosvitin approximately 72.73%. Furthermore, fraction F1 was separated on GFC to obtain two main sub-fractions (F1 and F2). Sub-fraction F1 from gel filtration was composed mostly of β-phosvitin with a high recovery rate (81.93%) while F2 was dominant with α-phosvitin in a lower phosvitin recovery rate (16.89%). These findings will provide useful information for further researches on other properties of phosvitin so that it can be applied widely in human needs.

scholarly journals Simultaneous purification of biotin-binding proteins-I and -II from chicken egg yolk and their characterization

1995 ◽  
Vol 308 (2) ◽  
pp. 573-577 ◽  
Author(s):  
N Subramanian ◽  
P R Adiga
Keyword(s):  
Physicochemical Properties ◽  
Affinity Chromatography ◽  
Binding Proteins ◽  
Egg Yolk ◽  
Cross Reactivity ◽  
Guanidinium Chloride ◽  
Chicken Egg ◽  
Butanol Extraction ◽  
Biotin Binding ◽  
Chicken Egg Yolk

Chicken egg yolk biotin-binding protein-I (BBP-I) has been purified to homogeneity along with the tetrameric BBP-II by a common protocol. The purification includes delipidation of egg yolk by butanol extraction, DEAE-Sephacel chromatography, treatment with guanidinium chloride and biotin-aminohexyl-Sepharose affinity chromatography. The identity of purified BBP-I was ascertained by its physicochemical properties as well as by its immunological cross-reactivity and precursor-product relationship with BBP-II.

scholarly journals Nature of the thiamin-binding protein from chicken egg yolk

1981 ◽  
Vol 193 (3) ◽  
pp. 679-685 ◽  
Author(s):  
K Muniyappa ◽  
P R Adiga
Keyword(s):  
Protein Fraction ◽  
Binding Capacity ◽  
Binding Protein ◽  
Deae Cellulose ◽  
Egg Yolk ◽  
Water Soluble ◽  
Molar Ratio ◽  
Ligand Interaction ◽  
Chicken Egg ◽  
Chicken Egg Yolk

A simple, rapid and efficient procedure for the purification of thiamin-binding protein from chicken egg yolk was developed. The method involved removal, by exclusion, of lipoproteins from DEAE-cellulose and subsequent elution of water-soluble proteins held on the ion-exchanger with 1 M-NaCl, followed by treatment of the eluted protein fraction with an aqueous suspension of dextran/charcoal to generate apoprotein from the holoprotein. The resultant protein fraction was subjected to bioaffinity chromatography on thiamin pyrophosphate–AE (aminoethyl)-Sepharose. The protein eluted specifically with 10 microM-thiamin at pH 7.0, was homogeneous by the criteria of polyacrylamide-gel disc electrophoresis, had a mol.wt. of 38 000 +/- 2000 and was not a glycoprotein. The purified thiamin-binding protein specifically interacted with riboflavin-binding protein with no detectable deleterious affect on its (14C)thiamin-binding capacity. The protein bound [14C]thiamin with a molar ratio of 1.0, with dissociation constant (Kd) 0.41 microM. This protein-ligand interaction was inhibited by thiamin analogues and antagonists. The absorption spectrum of the protein in the presence of thiamin exhibited significant hypochromism at the 278 nm band, indicating the involvement of aromatic amino acid residues of the protein, during its binding to the ligand. The protein cross-reacted with the monospecific antiserum to egg-white thiamin-binding protein, showing thereby that thiamin-binding proteins present in chicken egg yolk and white are the products of the same structural gene.

Chicken egg yolk antibodies (IgY)-based antivenom for neutralization of snake venoms: a review

Toxin Reviews ◽  
2021 ◽  
pp. 1-12
Author(s):  
Ankit Choraria ◽  
Rajeswari Somasundaram ◽  
S. Janani ◽  
Selvakumar Rajendran ◽  
Naoual Oukkache ◽  
...  
Keyword(s):  
Egg Yolk ◽  
Snake Venoms ◽  
Chicken Egg ◽  
Egg Yolk Antibodies ◽  
Chicken Egg Yolk
Sign in / Sign up

Export Citation Format

Share Document