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. 1970 Jul;118(3):537–542. doi: 10.1042/bj1180537

The isolation and composition of two phosphoproteins from hen's egg

R C Clark 1
PMCID: PMC1179223  PMID: 5528641

Abstract

1. Phosvitin extracted from domestic hen's-egg yolk was resolved on Sephadex G-100 into two phosphoprotein components. 2. The major component has a molecular weight of about 3.4×104 and alanine as an N-terminal residue. Glucosamine is present, but tyrosine is virtually absent. 3. The minor component has a molecular weight of about 2.8×104 and lysine as an N-terminal residue. Missing residues are glucosamine, methionine and leucine. Lysine, histidine, threonine, glycine, phenylalanine and tyrosine contents differ significantly from those of the major component. 4. Sephadex G-100 also removes small amounts of an impurity with a much higher molecular weight.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Allerton S. E., Perlmann G. E. Chemical characterization of the phosphoprotein phosvitin. J Biol Chem. 1965 Oct;240(10):3892–3898. [PubMed] [Google Scholar]
  2. CONNELLY C., TABORSKY G. Chromatographic fractionation of phosvitin. J Biol Chem. 1961 May;236:1364–1368. [PubMed] [Google Scholar]
  3. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  4. GRAY W. R., HARTLEY B. S. THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. Biochem J. 1963 Nov;89:379–380. doi: 10.1042/bj0890379. [DOI] [PubMed] [Google Scholar]
  5. Ho C., Magnuson J. A., Wilson J. B., Magnuson N. S., Kurland R. J. Phosphorus nuclear magnetic resonance studies of phosphoproteins and phosphorylated molecules. II. Chemical nature of phosphorus atoms in alpha S-casein B and phosvitin. Biochemistry. 1969 May;8(5):2074–2082. doi: 10.1021/bi00833a044. [DOI] [PubMed] [Google Scholar]
  6. JOUBERT F. J., COOK W. H. Preparation and characterization of phosvitin from hen egg yolk. Can J Biochem Physiol. 1958 Apr;36(4):399–408. [PubMed] [Google Scholar]
  7. JOUBERT F. J., COOK W. H. Separation and characterization of lipovitellin from hen egg yolk. Can J Biochem Physiol. 1958 Apr;36(4):389–398. [PubMed] [Google Scholar]
  8. Kawahara K., Tanford C. Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J Biol Chem. 1966 Jul 10;241(13):3228–3232. [PubMed] [Google Scholar]
  9. MOK C. C., MARTIN W. G., COMMON R. H. A comparison of phosvitins prepared from hen's serum and from hen's egg yolk. Can J Biochem Physiol. 1961 Jan;39:109–117. doi: 10.1139/o61-012. [DOI] [PubMed] [Google Scholar]
  10. MORRISON W. R. A FAST, SIMPLE AND RELIABLE METHOD FOR THE MICRODETERMINATION OF PHOSPHORUS IN BIOLOGICAL MATERIALS. Anal Biochem. 1964 Feb;7:218–224. doi: 10.1016/0003-2697(64)90231-3. [DOI] [PubMed] [Google Scholar]
  11. Mok C. C., Grant C. T., Taborsky G. Countercurrent distribution of phosvitin. Biochemistry. 1966 Aug;5(8):2517–2523. doi: 10.1021/bi00872a005. [DOI] [PubMed] [Google Scholar]
  12. SANGER F., THOMPSON E. O. Halogenation of tyrosine during acid hydrolysis. Biochim Biophys Acta. 1963 May 14;71:468–471. doi: 10.1016/0006-3002(63)91108-9. [DOI] [PubMed] [Google Scholar]
  13. TABORSKY G., ALLENDE C. C. A rearrangement in the structure of phosvitin. Biochemistry. 1962 May 25;1:406–411. doi: 10.1021/bi00909a006. [DOI] [PubMed] [Google Scholar]
  14. TABORSKY G. Interaction between phosvitin and iron and its effect on a rearrangement of phosvitin structure. Biochemistry. 1963 Mar-Apr;2:266–271. doi: 10.1021/bi00902a010. [DOI] [PubMed] [Google Scholar]
  15. Taborsky G., Mok C. C. Phosvitin. Homogeneity and molecular weight. J Biol Chem. 1967 Apr 10;242(7):1495–1501. [PubMed] [Google Scholar]
  16. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]

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