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 journalArticle

Abstract

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
Volume238
Issue number2
DOIs
StatePublished - May 1 1985

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Fibrinolysin
Divalent Cations
Fibrinogen
Digestion
Degradation
Binding Sites
Proteolysis
Dialysis
Electrophoresis
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Ions
Calcium
Molecules
fibrinogen D fragment

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Protective effect of divalent cations in the plasmin degradation of fibrinogen. / Dang, Chi V.; Bell, William R.; Ebert, Ray F.; Starksen, Niel F.

In: Archives of Biochemistry and Biophysics, Vol. 238, No. 2, 01.05.1985, p. 452-457.

Research output: Contribution to journalArticle

Dang, Chi V. ; Bell, William R. ; Ebert, Ray F. ; Starksen, Niel F. / Protective effect of divalent cations in the plasmin degradation of fibrinogen. In: Archives of Biochemistry and Biophysics. 1985 ; Vol. 238, No. 2. pp. 452-457.
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