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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
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Shaohui Wang et al.
The Journal of biological chemistry, 286(25), 22653-22664 (2011-05-03)
How fish embryos that develop externally survive microbial attacks is poorly understood. Here, we clearly demonstrated that the embryo extract of zebrafish and its early embryo both displayed antimicrobial activity against microbes, including pathogenic Aeromonas hydrophila, and phosvitin (Pv), a
Himali Samaraweera et al.
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
Khalil Abdelkebir et al.
Langmuir : the ACS journal of surfaces and colloids, 27(23), 14370-14379 (2011-10-20)
Layer-by-Layer (LbL) coatings are promising tools for the biofunctionalization of biomaterials, as they allow stress-free immobilization of proteins. Here, we explore the possibility to immobilize phosvitin, a highly phosphorylated protein viewed as a model of bone phosphoproteins and, as such
Jiandong Ren et al.
Food chemistry, 158, 186-191 (2014-04-16)
Egg yolk phosvitin serves as a warehouse to provide metal ions for embryo development. It is significant for mineral metabolism study and also of great potential to be developed into functional foods with mineral absorption promoting ability. In this study
Daniel S Schabacker et al.
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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