Phosvitin, a Phosphoprotein with Polyelectrolyte Characteristics

  • Gertrude E. Perlmann
  • Kärt Grizzuti


It is well established that phosphoproteins are widely distributed in all embryonic and developing tissue, and it has been suggested that several biological processes such as enzymic phosphoryl transfer or energy storage may involve the participation of the phosphorylated amino acid residues in these proteins (5, 13). Inasmuch as a knowledge of the chemistry and macromolecular conformation of phosphoproteins is an essential prerequisite for an understanding of how these materials enter metabolic processes, we have initiated a study on phosvitin, the phosphoprotein from hens’ egg yolk first isolated in 1949 by Mecham and Olcott (10). Although in our work chemical and physico-chemical techniques are used, we shall present here only some of the physicochemical studies currently carried out in our laboratory. We should like to show that the conformational characteristics of phosvitin are highly sensitive to pH and ionic strength and that this can best be explained by considering this protein as a polyelectrolyte.


Ionic Strength Circular Dichroism Intrinsic Viscosity Rotatory Dispersion Optical Rotatory Dispersion 
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Copyright information

© Plenum Press, New York 1970

Authors and Affiliations

  • Gertrude E. Perlmann
    • 1
  • Kärt Grizzuti
    • 1
  1. 1.The Rockefeller UniversityNew YorkUSA

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