Skip to main content

Abstract

Among the abnormal fibrinogens which we recently analyzed, two types of abnormality were found to have two structural defects: a genetically determined amino acid substitution and an additional secondary modification of the molecule due to the mutation (1, 2). Here we briefly describe these abnormal molecules.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Refeences

  1. S. Terukina, M. Matsuda, H. Hirata, Y. Takeda, T. Miyata, T. Takao and Y. Shimonishi, Substitution of γArg-275 by Cys in an abnormal fibrinogen “fibrinogen Osaka II.” Evidence for a unique solitary cystine structure at the mutation site, J. Biol. Chem., 263:13579 (1988).

    PubMed  CAS  Google Scholar 

  2. K. Yamazumi, K. Shimura, S. Terukina, N. Takahashi and M. Matsuda, A γ-methionine310 to threonine substitution and consequent N-glycosylation at γ asparagine-308 identified in a congenital dysfibrinogenemia associated with posttraumatic bleeding, fibrinogen Asahi, J. Clin. Invest., 83:1590 (1989).

    Article  PubMed  CAS  Google Scholar 

  3. M. Matsuda, M. Baba, K. Morimoto and C. Nakamikawa, Fibrinogen Tokyo II. An abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules, J. Clin. Invest., 72:1034 (1983).

    Article  PubMed  CAS  Google Scholar 

  4. P. P. Masci, A. N. Whitaker and D. J. Winzor, A simple chromatographic procedure for the purification of the D dimer fragment from cross-linked fibrin, Anal. Biochem., 147:128 (1985).

    Article  PubMed  CAS  Google Scholar 

  5. D. W. Chung, W.-Y. Chen and E. W. Davie, Characterization of a complementary deoxyribonucleic acid coding for the γ chain of human fibrinogen, Biochemistry, 22:3250 (1983).

    Article  PubMed  CAS  Google Scholar 

  6. M. W. Rixon, D. W. Chung and E. W. Davie, Nucleotide sequence of the gene for the γ chain of human fibrinogen, Biochemistry, 24:2077 (1985).

    Article  PubMed  CAS  Google Scholar 

  7. T. Takao, T. Hitouji, Y. Shimonishi, T. Tanabe, S. Inoue and M. Inoue, Verification of protein sequence by fast atom bombardment mass spectrometry. Amino acid sequence of protein S, a development-specific protein of myxococcus xanthus, J. Biol. Chem., 259:6105 (1984).

    PubMed  CAS  Google Scholar 

  8. C. Southan, A. Henschen and F. Lottspeich, The search for molecular defects in abnormal fibrinogens, in: “Fibrinogen, Recent Biochemical and Medical Aspects,” A. Henschen, H. Graeff and F. Lottspeich, eds., Walter de Gruyter, Berlin (1982).

    Google Scholar 

  9. T. Miyata, S. Terukina, M. Matsuda, A. Kasamatsu, Y. Takeda, T. Murakami and S. Iwanaga, Fibrinogens Kawaguchi and Osaka: An amino acid substitution of Aα arginine-16 to cysteine which forms an extra interchain disulfide bridge between the two Aα chains, J. Biochem., 102:93 (1987).

    PubMed  CAS  Google Scholar 

  10. M.-J. Rabiet, B. C. Furie and B. Furie, Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273, J. Biol. Chem., 261:15045 (1986).

    PubMed  CAS  Google Scholar 

  11. T. Koide, S. Odani, K. Takahashi, T. Ono and N. Sakuragawa, Antithrombin III Toyama: Replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability, Proc. Natl. Acad. Sci. USA,81:289 (1984).

    Article  PubMed  CAS  Google Scholar 

  12. N. Yoshida, K. Ota, M. Moroi and M. Matsuda, An apparently higher molecular weight γ-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of γ arginine-275 by cysteine, Blood, 71:480 (1988).

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1990 Springer Science+Business Media New York

About this chapter

Cite this chapter

Matsuda, M., Terukina, S., Yoshida, N., Yamazumi, K., Maekawa, H. (1990). Abnormal Fibrinogens with Two Structural Defects. In: Liu, C.Y., Chien, S. (eds) Fibrinogen, Thrombosis, Coagulation, and Fibrinolysis. Advances in Experimental Medicine and Biology, vol 281. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3806-6_6

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-3806-6_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6697-3

  • Online ISBN: 978-1-4615-3806-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics