Location of plasminogen-binding sites in human fibrin(ogen)

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Abstract

Affinity chromatography of various fibrinogen and fibrin fragments on Lys-plasminogen-Sepharose was used to localize the plasminogen-binding sites in human fibrin(ogen). The fragments studied in the present investigation were derived from the central (E) and the terminal (D) globular domains of fibrinogen and fibrin. Our results showed that these two different, sequentially nonidentical domains of fibrin(ogen) both carry plasminogen-binding sites. Competitive affinity chromatography of fragment D1 and fragments derived from it by proteolytic modification of its D γ-chain revealed that this modification causes an 11-fold increase of the association constant of the interaction with Lys-plasminogen-Sepharose. This suggests that the carboxy-terminal region of the D γ-chain is involved in controlling the plasminogen-binding site of the D domain. In contrast with its fragments, intact fibrinogen is not retained by Lys-plasminogen-Sepharose, indicating that the plasminogen-binding sites present in the constituent E and D domains are not fully functional in the parent molecule. It seems possible that the plasminogen-binding sites are present but hidden in fibrinogen and proteolytic dissection of the molecule uncovers these sites in E and D fragments by removing peptides masking the plasminogen-binding regions.

Original languageEnglish
Pages (from-to)2440-2446
Number of pages7
JournalBiochemistry
Volume22
Issue number10
Publication statusPublished - 1983

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Plasminogen
Fibrin
Binding Sites
Fibrinogen
Sepharose
Affinity chromatography
Affinity Chromatography
Dissection
Peptide Fragments
Molecules
estropipate
Association reactions
Peptides
lysyl-plasminogen
lysine-sepharose

ASJC Scopus subject areas

  • Biochemistry

Cite this

Location of plasminogen-binding sites in human fibrin(ogen). / Váradi, A.; Patthy, L.

In: Biochemistry, Vol. 22, No. 10, 1983, p. 2440-2446.

Research output: Contribution to journalArticle

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AB - Affinity chromatography of various fibrinogen and fibrin fragments on Lys-plasminogen-Sepharose was used to localize the plasminogen-binding sites in human fibrin(ogen). The fragments studied in the present investigation were derived from the central (E) and the terminal (D) globular domains of fibrinogen and fibrin. Our results showed that these two different, sequentially nonidentical domains of fibrin(ogen) both carry plasminogen-binding sites. Competitive affinity chromatography of fragment D1 and fragments derived from it by proteolytic modification of its D γ-chain revealed that this modification causes an 11-fold increase of the association constant of the interaction with Lys-plasminogen-Sepharose. This suggests that the carboxy-terminal region of the D γ-chain is involved in controlling the plasminogen-binding site of the D domain. In contrast with its fragments, intact fibrinogen is not retained by Lys-plasminogen-Sepharose, indicating that the plasminogen-binding sites present in the constituent E and D domains are not fully functional in the parent molecule. It seems possible that the plasminogen-binding sites are present but hidden in fibrinogen and proteolytic dissection of the molecule uncovers these sites in E and D fragments by removing peptides masking the plasminogen-binding regions.

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