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General description
Phosvitin from egg yolk is a polyanionic phosphoserine rich protein. This phosphoglycoprotein comprises α-helices and β-sheets structural elements, which are poorly organized due to the presence of phosphoserine. It represents about 11% of yolk proteins and is hydrophilic.
Application
Phosvitin from egg yolk has been used:
- as a control protein for immobilization on-chip for deep purple protein staining methods for monitoring post-translation modifications
- as a substrate for casein kinase Iε in in vitro casein kinase assay
- as a standard in gel filtration chromatography (GFC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) for quantification of phosvitin from egg extracts
- for immobilization onto Layer-by-Layer (LbL) for Fourier transform infrared spectroscopy-attenuated total reflectance (FTIR-ATR) studies
Biochem/physiol Actions
Phosvitin fed to rats by adding egg yolk to their food resulted in decreased absorption of magnesium, iron and calcium but not of phosphorus.
Phosvitin from egg yolk is a calcium chelator and binds to iron present in the yolk. The metal-binding functionality is exploited in mineral-binding bioactive peptide production. It is a nutraceutical and has potential for phosphopeptides production.
Other Notes
A phosophoprotein containing 8-10% phosphorus. Molar N/P ratio approx. 2.7.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Journal of food science, 76(7), R143-R150 (2011-08-03)
Phosphopeptides are among the most interesting biomolecules with characteristic molecular structure and functions. They usually contain clusters of phosphoserines, which can effectively bind calcium and iron, and inhibit formation of insoluble calcium phosphates or iron complexes. Therefore, phosphopeptides can increase
Food chemistry, 135(3), 993-998 (2012-09-08)
Phosvitin is a phosphoglycoprotein present in egg yolk. More than half of the amino acids in phosvitin molecule are serine, of which >90% are phosphorylated. Therefore, phosvitin has a strong metal binding capability. The aim of this study was to
Poultry science, 90(5), 1096-1104 (2011-04-15)
The objective of this study was to develop a new protocol that could be used for large-scale separation of phosvitin from egg yolk using ethanol and salts. Yolk granules, which contain phosvitin, were precipitated after diluting egg yolk with 9
Journal of biomedical materials research. Part A, 100(10), 2760-2765 (2012-05-25)
The aim of this study is to evaluate the mineralizing potential of acidic monomers and their calcium salts for mineralization, using an in vitro mineral induction model. Phosvitin (PV) was used as a model phosphoprotein in this study. PV was
Analytical biochemistry, 359(1), 84-93 (2006-10-13)
Methods to assess the quality and performance of protein microarrays fabricated from undefined protein content are required to elucidate slide-to-slide variability and interpolate resulting signal intensity values after an interaction assay. We therefore developed several simple total- and posttranslational modification-specific
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