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P1253

Sigma-Aldrich

Phosvitin from egg yolk

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About This Item

CAS Number:
9008-96-2
MDL number:
MFCD00131908
UNSPSC Code:
12352202
NACRES:
NA.81

biological source

egg yolk

form

powder

storage temp.

−20°C

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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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P1253-500MG:
P1253-1G:
P1253-50MG:
P1253-VAR:
P1253-BULK:
P1253-100MG:
P1253-250MG:

Certificates of Analysis (COA)

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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
Shuichi Ito et al.
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
Shuichi Ito et al.
Journal of dentistry, 39(1), 72-79 (2010-10-26)
The aim of this study was to evaluate the mineralizing potential of ions released from surface pre-reacted glass-ionomer (S-PRG) fillers on mineral induction by phosphoprotein in vitro. Phosvitin was used as a model of dentin phosphoprotein in this study. Phosvitin
S-I Ishikawa et al.
Journal of food science, 72(6), S412-S419 (2007-11-13)
Egg yolk decreases the absorption of iron. The effects of egg yolk protein and egg yolk phosvitin on the absorption of calcium, magnesium, and iron were investigated by in vivo studies. Male Wistar rats were fed purified diets containing casein
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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