Egg yolk phosvitin: preparation of metal-free purified protein by fast protein liquid chromatography using aqueous solvents.
Two chromatographic methods for hen egg yolk phosvitin purification avoiding organic solvents were evaluated. Hydrophobic interaction and ion-exchange chromatographies were applied to isolated phosvitin. Hydrophobic interaction chromatography has better capacity than ion-exchange chromatography to fractionate phosvitin in their different polypeptides, but its protein yield was lower (0.7 vs. 1.7% of egg yolk dry matter). Finally, ion-exchange chromatography was selected and allowed to fractionate phosvitin polypeptides, including the recovering of phosphoproteins with high electrophoretic mobility: phosvettes. Highly purified (>98%) and free metal protein was obtained in reduced time. Phosvitin polypeptide heterogeneity was evidenced.
Castellani
O
O
Laboratoire d'Etude des Interactions des Molécules Alimentaires, Institut National de la Recherche Agronomique, BP 71627, 44316 Nantes, Cedex 3, France.
Martinet
V
V
David-Briand
E
E
Guérin-Dubiard
C
C
Anton
M
M
D002852:Chromatography, Ion Exchange / Q000379:methods*; D004530:Egg Yolk / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D010774:Phosvitin / Q000302:isolation & purification*; D012997:Solvents / Q000737:chemistry*; D014867:Water
D012997:Solvents; D014867:Water; D010774:Phosvitin