Localization of a fibrin polymerization site complementary to Gly-His-Arg sequence

L. V. Medved, S. V. Litvinovich, T. P. Ugarova, N. I. Lukinova, V. N. Kalikhevich, Z. A. Ardemasova

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


Dansyl-labeled tetrapeptide Gly-His-Arg-Pro which mimics the central fibrin polymerization site was used to investigate its binding to a number of fibrinogen fragments containing different numbers of domains. The tetrapeptide was found to bind to fragments DH(95 kDa), DL(82 kDa) and DY(63 kDa) but not to the TSD(28 kDa) fragment. The DY fragment differs from the TSD by the presence of β and βC domains. Therefore these domains, which are formed by the C-terminal part of the β chain, possess a polymerization site complementary to the Gly-His-Arg containing counterpart.

Original languageEnglish (US)
Pages (from-to)239-242
Number of pages4
JournalFEBS Letters
Issue number3
StatePublished - Apr 12 1993
Externally publishedYes


  • Fibrin
  • Fibrinogen fragment
  • Polymerization site
  • Synthetic peptide

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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