β(Leu121-Lys122) segment of fibrinogen is in a region essential for plasminogen binding by fibrin fragment

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Abstract

It was shown previously that two sequentially nonidentical regions of human fibrin(ogen), present in fragments D and E, carry specific plasminogen-binding sites [Váradi, A., & Patthy, L. (1983) Biochemistry 22, 2440-2446]. Comparison of the affinity of a variety of fragment E species for immobilizd Lys-plasminogen revealed that fragment E3e [(α20/24-78, β54-122, γ1-53)2] possesses a strong plasminogen-binding site, whereas fragment E3t [(α20/24-78, β54-120, γ1-53)2] has 30-fold lower affinity for the affinant. Since the two fragments differ only in the β(Leu121-Lys122) segment, this suggests that residues β(Leu121-Lys122), present in the triple-helical connector region of fibrin(ogen), are essential for plasminogen binding by fragment E. Reduction and alkylation of fragment E3e lead to the destruction of the plasminogen-binding site, indicating that none of the separated, alkylated polypeptide chains of the fragment are able to bind to plasminogen and probably the coiled-coil superstructure of the connector region is necessary for the maintenance of the plasminogen-binding site of fragment E.

Original languageEnglish
Pages (from-to)2108-2112
Number of pages5
JournalBiochemistry
Volume23
Issue number9
Publication statusPublished - 1984

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Plasminogen
Fibrin
Fibrinogen
Binding Sites
Biochemistry
Alkylation
Maintenance
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "β(Leu121-Lys122) segment of fibrinogen is in a region essential for plasminogen binding by fibrin fragment",
abstract = "It was shown previously that two sequentially nonidentical regions of human fibrin(ogen), present in fragments D and E, carry specific plasminogen-binding sites [V{\'a}radi, A., & Patthy, L. (1983) Biochemistry 22, 2440-2446]. Comparison of the affinity of a variety of fragment E species for immobilizd Lys-plasminogen revealed that fragment E3e [(α20/24-78, β54-122, γ1-53)2] possesses a strong plasminogen-binding site, whereas fragment E3t [(α20/24-78, β54-120, γ1-53)2] has 30-fold lower affinity for the affinant. Since the two fragments differ only in the β(Leu121-Lys122) segment, this suggests that residues β(Leu121-Lys122), present in the triple-helical connector region of fibrin(ogen), are essential for plasminogen binding by fragment E. Reduction and alkylation of fragment E3e lead to the destruction of the plasminogen-binding site, indicating that none of the separated, alkylated polypeptide chains of the fragment are able to bind to plasminogen and probably the coiled-coil superstructure of the connector region is necessary for the maintenance of the plasminogen-binding site of fragment E.",
author = "Andr{\'a}s V{\'a}radi and L{\'a}szl{\'o} Patthy",
year = "1984",
language = "English",
volume = "23",
pages = "2108--2112",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "9",

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TY - JOUR

T1 - β(Leu121-Lys122) segment of fibrinogen is in a region essential for plasminogen binding by fibrin fragment

AU - Váradi, András

AU - Patthy, László

PY - 1984

Y1 - 1984

N2 - It was shown previously that two sequentially nonidentical regions of human fibrin(ogen), present in fragments D and E, carry specific plasminogen-binding sites [Váradi, A., & Patthy, L. (1983) Biochemistry 22, 2440-2446]. Comparison of the affinity of a variety of fragment E species for immobilizd Lys-plasminogen revealed that fragment E3e [(α20/24-78, β54-122, γ1-53)2] possesses a strong plasminogen-binding site, whereas fragment E3t [(α20/24-78, β54-120, γ1-53)2] has 30-fold lower affinity for the affinant. Since the two fragments differ only in the β(Leu121-Lys122) segment, this suggests that residues β(Leu121-Lys122), present in the triple-helical connector region of fibrin(ogen), are essential for plasminogen binding by fragment E. Reduction and alkylation of fragment E3e lead to the destruction of the plasminogen-binding site, indicating that none of the separated, alkylated polypeptide chains of the fragment are able to bind to plasminogen and probably the coiled-coil superstructure of the connector region is necessary for the maintenance of the plasminogen-binding site of fragment E.

AB - It was shown previously that two sequentially nonidentical regions of human fibrin(ogen), present in fragments D and E, carry specific plasminogen-binding sites [Váradi, A., & Patthy, L. (1983) Biochemistry 22, 2440-2446]. Comparison of the affinity of a variety of fragment E species for immobilizd Lys-plasminogen revealed that fragment E3e [(α20/24-78, β54-122, γ1-53)2] possesses a strong plasminogen-binding site, whereas fragment E3t [(α20/24-78, β54-120, γ1-53)2] has 30-fold lower affinity for the affinant. Since the two fragments differ only in the β(Leu121-Lys122) segment, this suggests that residues β(Leu121-Lys122), present in the triple-helical connector region of fibrin(ogen), are essential for plasminogen binding by fragment E. Reduction and alkylation of fragment E3e lead to the destruction of the plasminogen-binding site, indicating that none of the separated, alkylated polypeptide chains of the fragment are able to bind to plasminogen and probably the coiled-coil superstructure of the connector region is necessary for the maintenance of the plasminogen-binding site of fragment E.

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