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

doi:10.1016/0014-5793(93)80594-K

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 journal › Article › peer-review

22 Scopus citations

Abstract

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 D_H(95 kDa), D_L(82 kDa) and D_Y(63 kDa) but not to the TSD(28 kDa) fragment. The D_Y 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 language	English (US)
Pages (from-to)	239-242
Number of pages	4
Journal	FEBS Letters
Volume	320
Issue number	3
DOIs	https://doi.org/10.1016/0014-5793(93)80594-K
State	Published - Apr 12 1993
Externally published	Yes

Keywords

Fibrin
Fibrinogen fragment
Polymerization site
Synthetic peptide

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(93)80594-K

Cite this

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title = "Localization of a fibrin polymerization site complementary to Gly-His-Arg sequence",

abstract = "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.",

keywords = "Fibrin, Fibrinogen fragment, Polymerization site, Synthetic peptide",

author = "Medved, {L. V.} and Litvinovich, {S. V.} and Ugarova, {T. P.} and Lukinova, {N. I.} and Kalikhevich, {V. N.} and Ardemasova, {Z. A.}",

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T1 - Localization of a fibrin polymerization site complementary to Gly-His-Arg sequence

AU - Medved, L. V.

AU - Litvinovich, S. V.

AU - Ugarova, T. P.

AU - Lukinova, N. I.

AU - Kalikhevich, V. N.

AU - Ardemasova, Z. A.

PY - 1993/4/12

Y1 - 1993/4/12

N2 - 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.

AB - 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.

KW - Fibrin

KW - Fibrinogen fragment

KW - Polymerization site

KW - Synthetic peptide

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

Abstract

Keywords

ASJC Scopus subject areas

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