Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 15 (1), 1-9

Oligophosphopeptides of Varied Structural Complexity Derived From the Egg Phosphoprotein, Phosvitin

Affiliations

Oligophosphopeptides of Varied Structural Complexity Derived From the Egg Phosphoprotein, Phosvitin

A Goulas et al. J Protein Chem.

Abstract

Phosvitins are the principal phosphoproteins in the eggs of oviparous vertebrates. They have an exceptionally high serine content and most, or even all, of the serine residues are esterified to phosphate. The phosphorylated residues tend to occur in uninterrupted runs of as many as 28 phosphoserines (as in Xenopus phosvitin). This unique structural feature gives phosvitins extraordinary properties and can be expected to play a key role in phosvitin function. For example, the concentration of phosphate groups provides for numerous highly efficient metal-binding sites in clusters. The mode of binding had been shown to be affected by the size of the protein and the degree to which serine residues are phosphorylated. For structure-function studies of phosvitins (and other polyphosphoproteins), phosphopeptides of differentiated structural complexity are desirable. Such model peptides were produced in this work by limited proteolysis of chicken phosvitin, and oligophosphopeptides of widely varying sizes, phosphoserine content, and sequence were purified and characterized. These include phosvitin segments containing one, two, or several oligophosphoserine runs, corresponding to segments of the N-terminal, C-terminal, and core sequence of the protein.

Similar articles

See all similar articles

Cited by 6 PubMed Central articles

See all "Cited by" articles

References

    1. Biochem J. 1970 Jul;118(3):537-42 - PubMed
    1. J Inorg Biochem. 1987 Jan;29(1):33-47 - PubMed
    1. Nucleic Acids Res. 1987 Jun 25;15(12):4737-60 - PubMed
    1. Comp Biochem Physiol B. 1990;96(4):655-63 - PubMed
    1. Can J Biochem Physiol. 1958 Apr;36(4):399-408 - PubMed

Publication types

LinkOut - more resources

Feedback