Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Sep;76(9):4327–4330. doi: 10.1073/pnas.76.9.4327

Identification of gamma-glutamyl phosphate in the alpha 2 chains of chicken bone collagen.

L Cohen-Solal, M Cohen-Solal, M J Glimcher
PMCID: PMC411567  PMID: 291967

Abstract

Purified components of chicken bone collagen contain approximately 4 atoms of organic phosphorus per mol of collagen, located principally in the alpha 2 chains. Previous analyses have demonstrated the absence of O-phosphoserine, O-phosphothreonine, and other phosphorylated hydroxy amino acids, phosphoamidated amino acids, and phosphorylated sugars. In the present report we establish that chicken bone collagen contains gamma-glutamyl phosphate. This was accomplished by the isolation of tritiated alpha-amino-delta-hydroxyvaleric acid after reductive cleavage with NaB[3H]H4 of the gamma components, the alpha 2 chains, and peptides enriched in organic phosphorus that were derived from the alpha 2 chains. Tritiated alpha-amino-delta-hydroxyvaleric acid was not detected in any of the following unphosphorylated proteins after cleavage with NaB[3H]H4:albumin and lysozyme, the alpha 2 chains of several unmineralized tissues, and, most importantly, dephosphorylated alpha 2 chains of chicken bone collagen. The alpha 2 chain of chicken bone collagen is the first structural protein found to contain an acyl phosphate.

Full text

PDF
4327

Selected References

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

  1. Anthony R. S., Spector L. B. A phosphoenzyme intermediary in acetate kinase action. J Biol Chem. 1970 Dec 25;245(24):6739–6741. [PubMed] [Google Scholar]
  2. Anthony R. S., Spector L. B. Phosphorylated acetate kinase. Its isolation and reactivity. J Biol Chem. 1972 Apr 10;247(7):2120–2125. [PubMed] [Google Scholar]
  3. Cohen-Solal L., Lian J. B., Kossiva D., Glimcher M. J. Identification of organic phosphorus covalently bound to collagen and non-collagenous proteins of chicken-bone matrix. The presence of O-phosphoserine and O-phosphothreonine in non-collagenous proteins, and their absence from phosporylated collagen. Biochem J. 1979 Jan 1;177(1):81–98. doi: 10.1042/bj1770081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cohen-Solal L., Lian J. B., Kossiva D., Glimcher M. J. The identification of O-phosphothreonine in the soluble non-collagenous phosphoproteins of bone matrix. FEBS Lett. 1978 May 1;89(1):107–110. doi: 10.1016/0014-5793(78)80533-x. [DOI] [PubMed] [Google Scholar]
  5. Degani C., Boyer P. D. A borohydride reduction method for characterization of the acyl phosphate linkage in proteins and its application to sarcoplasmic reticulum adenosine triphosphatase. J Biol Chem. 1973 Dec 10;248(23):8222–8226. [PubMed] [Google Scholar]
  6. GLIMCHER M. J., KRANE S. M. THE INCORPORATION OF RADIOACTIVE INORGANIC ORTHOPHOSPHATE AS ORGANIC PHOSPHATE BY COLLAGEN FIBRILS IN VITRO. Biochemistry. 1964 Feb;3:195–202. doi: 10.1021/bi00890a010. [DOI] [PubMed] [Google Scholar]
  7. Gilmcher M. J., Katz E. P. The organization of collagen in bone: the role of noncovalent bonds in the relative insolubility of bone collagen. J Ultrastruct Res. 1965 Jun;12(5):705–729. doi: 10.1016/s0022-5320(65)80057-0. [DOI] [PubMed] [Google Scholar]
  8. Nagano K., Kanazawa T., Mizuno N., Tashima Y., Nakao T., Nakao M. Some acyl phosphate-like properties of P32-labeled sodium-potassium-activated adenosine triphosphatase. Biochem Biophys Res Commun. 1965 Jun 9;19(6):759–764. doi: 10.1016/0006-291x(65)90324-4. [DOI] [PubMed] [Google Scholar]
  9. Nishigaki I., Chen F. T., Hokin L. E. Studies on the characterization of the sodium-potassium transport adenosine triphosphatase. XV. Direct chemical characterization of the acyl phosphate in the enzyme as an aspartyl beta-phosphate residue. J Biol Chem. 1974 Aug 10;249(15):4911–4916. [PubMed] [Google Scholar]
  10. PIEZ K. A., MORRIS L. A modified procedure for the automatic analysis of amino acids. Anal Biochem. 1960 Nov;1:187–201. doi: 10.1016/0003-2697(60)90045-2. [DOI] [PubMed] [Google Scholar]
  11. Seyer J., Glimcher M. J. The amino acid sequence of two O-phosphoserine containing tripeptides isolated from the organic matrix of embryonic bovine enamel. Biochim Biophys Acta. 1969 Jul 1;181(2):410–418. doi: 10.1016/0005-2795(69)90274-8. [DOI] [PubMed] [Google Scholar]
  12. Spector A. R., Glimcher M. J. The identification of O-phosphoserine in the soluble anionic phosphoproteins of bone. Biochim Biophys Acta. 1973 Apr 20;303(2):360–362. doi: 10.1016/0005-2795(73)90367-x. [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. Phosphoproteins. Adv Protein Chem. 1974;28:1–210. doi: 10.1016/s0065-3233(08)60230-2. [DOI] [PubMed] [Google Scholar]
  16. Todhunter J. A., Purich D. L. Evidence for the formation of a gamma-phosphorylated glutamyl residue in the Escherichia coli acetate kinase reaction. Biochem Biophys Res Commun. 1974 Sep 9;60(1):273–280. doi: 10.1016/0006-291x(74)90201-0. [DOI] [PubMed] [Google Scholar]
  17. Walsh C. T., Jr, Hildebrand J. G., Spector L. B. Succinyl phosphate. Its nonenzymatic hydrolysis and reaction with coenzyme A. J Biol Chem. 1970 Nov 10;245(21):5699–5708. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES