Comparative study of hen yolk phosvitin and plasma vitellogenin

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Abstract
Vitellogenin, the only phosphoprotein detectable in the plasma of laying hens, was present at an approximate concentration of 1 mg/ml and was isolated by chromatography of DEAE cellulose. Vitellogenin had a MW of 235,000-240,000 and contained approximately 3% P by weight. Evidence that this protein was the precursor of phosvitins included its ability to act as an acceptor for phosphate with a phosvitin specific kinase, the generation of a peptide similar to phosvitin by trypsinization and the presence of distinctive peptides of multiple clustered phosphoserine upon partial acid hydrolysis. This partial sequence similarity between phosvitins and vitellogenin was not previously reported. The P content and amino acid composition of vitellogenin were consistent with a model which contains 2 phosvitins and 1 lipovitellin. The total MW of these proteins (28,000 + 34,000 + 170,000 = 232,000) were close to that of vitellogenin.

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