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

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.

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

Biochemical Journal ◽

10.1042/bj1570395 ◽

1976 ◽

Vol 157 (2) ◽

pp. 395-400 ◽

Cited By ~ 38

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.

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Purification of biotin-binding protein from chicken egg yolk and comparison with avidin

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(84)90092-x ◽

1984 ◽

Vol 786 (3) ◽

pp. 222-230 ◽

Cited By ~ 14

Author(s):

C.V. Ramana Murthy ◽

P. Radhakantha Adiga

Keyword(s):

Binding Protein ◽

Egg Yolk ◽

Chicken Egg ◽

Biotin Binding ◽

Chicken Egg Yolk

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Detection of Hazelnut Proteins in Foods by Enzyme Immunoassay Using Egg Yolk Antibodies

Journal of Food Protection ◽

10.4315/0362-028x-64.6.895 ◽

2001 ◽

Vol 64 (6) ◽

pp. 895-898 ◽

Cited By ~ 26

Author(s):

BURTON W. BLAIS ◽

LUCILLE PHILLIPPE

Keyword(s):

Enzyme Immunoassay ◽

Food Industry ◽

Egg Yolk ◽

Cross Reactivity ◽

Regulatory Agencies ◽

Chicken Egg ◽

Egg Yolk Antibodies ◽

Food Matrices ◽

Chicken Egg Yolk

An enzyme immunoassay (EIA) was developed for the detection of hazelnut proteins in foods. This assay used inexpensive chicken egg yolk antibodies in a sandwich EIA format for the immunospecific capture and detection of hazelnut proteins present in a variety of different food matrices. The assay was able to detect less than 1 ppm of hazelnut protein in most of the foods tested and did not exhibit any appreciable cross-reactivity with other nuts or food matrices. This assay will be a useful tool for the food industry and regulatory agencies that wish to test foods for the presence of undeclared hazelnut allergens.

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