Protective effect of divalent cations in the plasmin degradation of fibrinogen

Chi V. Dang, William R. Bell, Ray F. Ebert, Niel F. Starksen

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Calcium limits the plasmic proteolysis of fibrinogen fragment D by binding to a specific site on the carboxy-terminal segment of the Dγ chain. Employing sodium dodecyl sulfate-polyacrylamide gel electrophoresis to visualize plasmic fragments, Sr2+, Ba2+, and Mn2+ were found to have an equivalent capacity to limit the degradation of fibrinogen fragment D (Mr 94,000). Mg2+, Fe2+, Co2+, and Zn2+ did not comparably limit the digestion of fragment D. Equilibrium dialysis demonstrated that Ba2+ competitively inhibited Ca2+ binding to fibrinogen, suggesting that the ions occupied the Ca2+ binding site of fibrinogen and thereby limited the plasmic digestion of fragment D. The results suggest that Ca2+, Sr2+, Ba2+, and Mn2+ limit plasmin digestion of fragment D by interacting with a Ca2+ binding site in the D domain of the fibrinogen molecule.

Original languageEnglish (US)
Pages (from-to)452-457
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - May 1 1985

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry


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