P1253
Phosvitin from egg yolk
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About This Item
Prodotti consigliati
Origine biologica
egg yolk
Forma fisica
powder
Temperatura di conservazione
−20°C
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Descrizione generale
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.
Applicazioni
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
Azioni biochim/fisiol
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.
Altre note
A phosophoprotein containing 8-10% phosphorus. Molar N/P ratio approx. 2.7.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
Certificati d'analisi (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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