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
. 1976 Oct;73(10):3374–3375. doi: 10.1073/pnas.73.10.3374

Primary structure of the gamma-carboxyglutamic acid-containing protein from bovine bone.

P A Price, J W Poser, N Raman
PMCID: PMC431116  PMID: 1068450

Abstract

The amino-acid sequence of the gamma-carboxyglutamic acid-containing protein of bovine bone is presented. The sequence of 43 of the 49 residues was determined automatically on the intact protein and on a tryptic peptide. The remainder was determined by conventional procedures on tryptic and chymotrytic peptides. Residue 9 in the sequence has been identified as 4-hydroxyproline. The protein contains three gamma-carboxyglutamic acid residues, which are located at positions 17, 21, and 24. The role of these unusual amino acids in the binding interaction between the protein and hydroxyapatite crystals is discussed.

Full text

PDF
3374

Selected References

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

  1. Atassi M. Z., Caruso D. R. Immunochemistry of sperm whale myoglobin. II. Modification of the two tryptophan residues and their role in the conformation and antigen-antibody reaction. Biochemistry. 1968 Feb;7(2):699–705. doi: 10.1021/bi00842a027. [DOI] [PubMed] [Google Scholar]
  2. Betts F., Blumenthal N. C., Posner A. S., Becker G. L., Lehninger A. L. Atomic structure of intracellular amorphous calcium phosphate deposits. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2088–2090. doi: 10.1073/pnas.72.6.2088. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bruton C. J., Hartley B. S. Chemical studies on methionyl-tRNA synthetase from Escherichia coli. J Mol Biol. 1970 Sep 14;52(2):165–178. doi: 10.1016/0022-2836(70)90023-9. [DOI] [PubMed] [Google Scholar]
  4. Enfield D. L., Ericsson L. H., Walsh K. A., Neurath H., Titani K. Bovine factor X1 (Stuart factor). Primary structure of the light chain. Proc Natl Acad Sci U S A. 1975 Jan;72(1):16–19. doi: 10.1073/pnas.72.1.16. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Fietzek P. P., Rexrodt F. W., Wendt P., Stark M., Kühn K. The covalent structure of collagen. Amino-acid sequence of peptide 1-CB6-C2. Eur J Biochem. 1972 Oct 17;30(1):163–168. doi: 10.1111/j.1432-1033.1972.tb02083.x. [DOI] [PubMed] [Google Scholar]
  6. Hauschka P. V., Lian J. B., Gallop P. M. Direct identification of the calcium-binding amino acid, gamma-carboxyglutamate, in mineralized tissue. Proc Natl Acad Sci U S A. 1975 Oct;72(10):3925–3929. doi: 10.1073/pnas.72.10.3925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hermodson M. A., Ericsson L. H., Titani K., Neurath H., Walsh K. A. Application of sequenator analyses to the study of proteins. Biochemistry. 1972 Nov 21;11(24):4493–4502. doi: 10.1021/bi00774a011. [DOI] [PubMed] [Google Scholar]
  8. Howard J. B., Nelsestuen G. L. Isolation and characterization of vitamin K-dependent region of bovine blood clotting factor X. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1281–1285. doi: 10.1073/pnas.72.4.1281. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Magnusson S., Sottrup-Jensen L., Petersen T. E., Morris H. R., Dell A. Primary structure of the vitamin K-dependent part of prothrombin. FEBS Lett. 1974 Aug 25;44(2):189–193. doi: 10.1016/0014-5793(74)80723-4. [DOI] [PubMed] [Google Scholar]
  10. Mendez E., Lai C. Y. Regeneration of amino acids from thiazolinones formed in the Edman degradation. Anal Biochem. 1975 Sep;68(1):47–53. doi: 10.1016/0003-2697(75)90677-6. [DOI] [PubMed] [Google Scholar]
  11. Nelsestuen G. L., Broderius M., Zytkovicz T. H., Howard J. B. On the role of gamma-carboxyglutamic acid in calcium and phospholipid binding. Biochem Biophys Res Commun. 1975 Jul 8;65(1):233–240. doi: 10.1016/s0006-291x(75)80084-2. [DOI] [PubMed] [Google Scholar]
  12. Price P. A., Otsuka A. A., Poser J. W., Kristaponis J., Raman N. Characterization of a gamma-carboxyglutamic acid-containing protein from bone. Proc Natl Acad Sci U S A. 1976 May;73(5):1447–1451. doi: 10.1073/pnas.73.5.1447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Steiner D. F., Kemmler W., Tager H. S., Peterson J. D. Proteolytic processing in the biosynthesis of insulin and other proteins. Fed Proc. 1974 Oct;33(10):2105–2115. [PubMed] [Google Scholar]
  14. Summers M. R., Smythers G. W., Oroszlan S. Thin-layer chromatography of sub-nanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets. Anal Biochem. 1973 Jun;53(2):624–628. doi: 10.1016/0003-2697(73)90114-0. [DOI] [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