Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1987 Aug 1;245(3):887–891. doi: 10.1042/bj2450887

Disulphide bridges of bovine factor X.

P Højrup 1, S Magnusson 1
PMCID: PMC1148212  PMID: 3663198

Abstract

Evidence is presented for the disulphide bridges in bovine Factor X. The protein was degraded by chemical and enzymic means, and all 12 disulphide bridges were isolated in separate peptides except for bridges nos. 6/7 in the light chain. All the disulphide bridges were found to be in positions corresponding to those found in other homologous domains. This report is the first verification of an epidermal-growth-factor-homologous domain having the same disulphide-bonding pattern as that found in mouse epidermal growth factor.

Full text

PDF
888

Selected References

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

  1. Blomquist M. C., Hunt L. T., Barker W. C. Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7363–7367. doi: 10.1073/pnas.81.23.7363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cool D. E., Edgell C. J., Louie G. V., Zoller M. J., Brayer G. D., MacGillivray R. T. Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa. J Biol Chem. 1985 Nov 5;260(25):13666–13676. [PubMed] [Google Scholar]
  3. Dahlbäck B., Lundwall A., Stenflo J. Primary structure of bovine vitamin K-dependent protein S. Proc Natl Acad Sci U S A. 1986 Jun;83(12):4199–4203. doi: 10.1073/pnas.83.12.4199. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dode C., Rabiet M. J., Bertrand O., Labie D., Elion J. Characterization of a proteolytically modified form of human prothorombin. Biochem Biophys Res Commun. 1980 May 30;94(2):660–666. doi: 10.1016/0006-291x(80)91283-8. [DOI] [PubMed] [Google Scholar]
  5. Doolittle R. F., Feng D. F., Johnson M. S. Computer-based characterization of epidermal growth factor precursor. Nature. 1984 Feb 9;307(5951):558–560. doi: 10.1038/307558a0. [DOI] [PubMed] [Google Scholar]
  6. Enfield D. L., Ericsson L. H., Fujikawa K., Walsh K. A., Neurath H., Titani K. Amino acid sequence of the light chain of bovine factor X1 (Stuart factor). Biochemistry. 1980 Feb 19;19(4):659–667. doi: 10.1021/bi00545a009. [DOI] [PubMed] [Google Scholar]
  7. Esmon N. L., DeBault L. E., Esmon C. T. Proteolytic formation and properties of gamma-carboxyglutamic acid-domainless protein C. J Biol Chem. 1983 May 10;258(9):5548–5553. [PubMed] [Google Scholar]
  8. Foster D. C., Yoshitake S., Davie E. W. The nucleotide sequence of the gene for human protein C. Proc Natl Acad Sci U S A. 1985 Jul;82(14):4673–4677. doi: 10.1073/pnas.82.14.4673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fung M. R., Hay C. W., MacGillivray R. T. Characterization of an almost full-length cDNA coding for human blood coagulation factor X. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3591–3595. doi: 10.1073/pnas.82.11.3591. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Günzler W. A., Steffens G. J., Otting F., Kim S. M., Frankus E., Flohé L. The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain. Hoppe Seylers Z Physiol Chem. 1982 Oct;363(10):1155–1165. doi: 10.1515/bchm2.1982.363.2.1155. [DOI] [PubMed] [Google Scholar]
  11. Hagen F. S., Gray C. L., O'Hara P., Grant F. J., Saari G. C., Woodbury R. G., Hart C. E., Insley M., Kisiel W., Kurachi K. Characterization of a cDNA coding for human factor VII. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2412–2416. doi: 10.1073/pnas.83.8.2412. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hunt L. T., Barker W. C., Dayhoff M. O. Epidermal growth factor: internal duplication and probable relationship to pancreatic secretory trypsin inhibitor. Biochem Biophys Res Commun. 1974 Oct 8;60(3):1020–1028. doi: 10.1016/0006-291x(74)90415-x. [DOI] [PubMed] [Google Scholar]
  13. Højrup P., Jensen M. S., Petersen T. E. Amino acid sequence of bovine protein Z: a vitamin K-dependent serine protease homolog. FEBS Lett. 1985 May 20;184(2):333–338. doi: 10.1016/0014-5793(85)80633-5. [DOI] [PubMed] [Google Scholar]
  14. Katayama K., Ericsson L. H., Enfield D. L., Walsh K. A., Neurath H., Davie E. W., Titani K. Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas Factor) with that of other vitamin K-dependent plasma proteins. Proc Natl Acad Sci U S A. 1979 Oct;76(10):4990–4994. doi: 10.1073/pnas.76.10.4990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Leytus S. P., Chung D. W., Kisiel W., Kurachi K., Davie E. W. Characterization of a cDNA coding for human factor X. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3699–3702. doi: 10.1073/pnas.81.12.3699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lim T. K., Bloomfield V. A., Nelsestuen G. L. Structure of the prothrombin- and blood clotting factor X-membrane complexes. Biochemistry. 1977 Sep 20;16(19):4177–4181. doi: 10.1021/bi00638a007. [DOI] [PubMed] [Google Scholar]
  17. McMullen B. A., Fujikawa K., Kisiel W., Sasagawa T., Howald W. N., Kwa E. Y., Weinstein B. Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. Biochemistry. 1983 Jun 7;22(12):2875–2884. doi: 10.1021/bi00281a016. [DOI] [PubMed] [Google Scholar]
  18. Pennica D., Holmes W. E., Kohr W. J., Harkins R. N., Vehar G. A., Ward C. A., Bennett W. F., Yelverton E., Seeburg P. H., Heyneker H. L. Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature. 1983 Jan 20;301(5897):214–221. doi: 10.1038/301214a0. [DOI] [PubMed] [Google Scholar]
  19. Petersen T. E., Thłgersen H. C., Sottrup-Jensen L., Magnusson S., Jörnvall H. Isolation and N-terminal amino acid sequence of protein Z, a gamma-carboxyglutamic acid containing protein from bovine plasma. FEBS Lett. 1980 Jun 2;114(2):278–282. doi: 10.1016/0014-5793(80)81133-1. [DOI] [PubMed] [Google Scholar]
  20. Russell D. W., Schneider W. J., Yamamoto T., Luskey K. L., Brown M. S., Goldstein J. L. Domain map of the LDL receptor: sequence homology with the epidermal growth factor precursor. Cell. 1984 Jun;37(2):577–585. doi: 10.1016/0092-8674(84)90388-x. [DOI] [PubMed] [Google Scholar]
  21. Savage C. R., Jr, Hash J. H., Cohen S. Epidermal growth factor. Location of disulfide bonds. J Biol Chem. 1973 Nov 25;248(22):7669–7672. [PubMed] [Google Scholar]
  22. Sugo T., Björk I., Holmgren A., Stenflo J. Calcium-binding properties of bovine factor X lacking the gamma-carboxyglutamic acid-containing region. J Biol Chem. 1984 May 10;259(9):5705–5710. [PubMed] [Google Scholar]
  23. Südhof T. C., Goldstein J. L., Brown M. S., Russell D. W. The LDL receptor gene: a mosaic of exons shared with different proteins. Science. 1985 May 17;228(4701):815–822. doi: 10.1126/science.2988123. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Thøgersen H. C., Petersen T. E., Sottrup-Jensen L., Magnusson S., Morris H. R. The N-terminal sequences of blood coagulation factor X1 and X2 light chains. Mass-spectrometric identification of twelve residues of gamma-carboxyglutamic acid in their vitamin K-dependent domains. Biochem J. 1978 Nov 1;175(2):613–627. doi: 10.1042/bj1750613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Titani K., Fujikawa K., Enfield D. L., Ericsson L. H., Walsh K. A., Neurath H. Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain. Proc Natl Acad Sci U S A. 1975 Aug;72(8):3082–3086. doi: 10.1073/pnas.72.8.3082. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Tuhy P. M., Bloom J. W., Mann K. G. Decarboxylation of bovine prothrombin fragment 1 and prothrombin. Biochemistry. 1979 Dec 25;18(26):5842–5848. doi: 10.1021/bi00593a014. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES