Vzaimodeǐstvie analoga tsentra E1-tetrapeptida Gly-Pro-Arg-Pro s tsentrom D1 dvukh form monomernogo fibrina.

Translated title of the contribution: Interaction of an analog of the E1 site of tetrapeptide Gly-Pro-Arg-Pro with the D1 site of two forms of monomeric fibrin

Tatiana Ugarova, V. P. Romanova, V. A. Belitser

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Two monomeric fibrin forms differing in a set of polymerization sites (fibrin desAA and fibrin-desAABB) are inhibited to a different extent by tetrapeptide Gly-Pro-Arg-Pro which simulates a moiety of polymerization site E1. The lesser sensitivity of fibrin-desAABB polymerization to the inhibiting tetrapeptide is due to the presence of active site E2 in it. A shape of the concentration dependence curve of the inhibitory effect of tetrapeptide Gly-Pro-Arg-Pro on the polymerization of both fibrin types is similar to the previously found curve for fibrinogen and its fragments--specific inhibitors of polymerization. Ca2+ intensifies inhibition of fibrin-desAABB polymerization by tetrapeptide Gly-Pro-Arg-Pro twice as much as that of fibrin-desAA evidently due to the peptide blockage of sites D2. An increase of the ionic strength from 0.15 to 0.3 enhances the inhibitory effect of the tetrapeptide on polymerization of two monomeric fibrin forms.

Original languageUndefined/Unknown
Pages (from-to)3-9
Number of pages7
JournalUkrainskii biokhimicheskii zhurnal
Volume58
Issue number2
StatePublished - Mar 1986
Externally publishedYes

Fingerprint

glycyl-prolyl-arginyl-proline
Fibrin
Polymerization
glycyl-prolyl-arginyl-valyl-valyl-glutamic acid
Ionic strength
Osmolar Concentration
Fibrinogen
Catalytic Domain

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry

Cite this

Vzaimodeǐstvie analoga tsentra E1-tetrapeptida Gly-Pro-Arg-Pro s tsentrom D1 dvukh form monomernogo fibrina. / Ugarova, Tatiana; Romanova, V. P.; Belitser, V. A.

In: Ukrainskii biokhimicheskii zhurnal, Vol. 58, No. 2, 03.1986, p. 3-9.

Research output: Contribution to journalArticle

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abstract = "Two monomeric fibrin forms differing in a set of polymerization sites (fibrin desAA and fibrin-desAABB) are inhibited to a different extent by tetrapeptide Gly-Pro-Arg-Pro which simulates a moiety of polymerization site E1. The lesser sensitivity of fibrin-desAABB polymerization to the inhibiting tetrapeptide is due to the presence of active site E2 in it. A shape of the concentration dependence curve of the inhibitory effect of tetrapeptide Gly-Pro-Arg-Pro on the polymerization of both fibrin types is similar to the previously found curve for fibrinogen and its fragments--specific inhibitors of polymerization. Ca2+ intensifies inhibition of fibrin-desAABB polymerization by tetrapeptide Gly-Pro-Arg-Pro twice as much as that of fibrin-desAA evidently due to the peptide blockage of sites D2. An increase of the ionic strength from 0.15 to 0.3 enhances the inhibitory effect of the tetrapeptide on polymerization of two monomeric fibrin forms.",
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T1 - Vzaimodeǐstvie analoga tsentra E1-tetrapeptida Gly-Pro-Arg-Pro s tsentrom D1 dvukh form monomernogo fibrina.

AU - Ugarova, Tatiana

AU - Romanova, V. P.

AU - Belitser, V. A.

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N2 - Two monomeric fibrin forms differing in a set of polymerization sites (fibrin desAA and fibrin-desAABB) are inhibited to a different extent by tetrapeptide Gly-Pro-Arg-Pro which simulates a moiety of polymerization site E1. The lesser sensitivity of fibrin-desAABB polymerization to the inhibiting tetrapeptide is due to the presence of active site E2 in it. A shape of the concentration dependence curve of the inhibitory effect of tetrapeptide Gly-Pro-Arg-Pro on the polymerization of both fibrin types is similar to the previously found curve for fibrinogen and its fragments--specific inhibitors of polymerization. Ca2+ intensifies inhibition of fibrin-desAABB polymerization by tetrapeptide Gly-Pro-Arg-Pro twice as much as that of fibrin-desAA evidently due to the peptide blockage of sites D2. An increase of the ionic strength from 0.15 to 0.3 enhances the inhibitory effect of the tetrapeptide on polymerization of two monomeric fibrin forms.

AB - Two monomeric fibrin forms differing in a set of polymerization sites (fibrin desAA and fibrin-desAABB) are inhibited to a different extent by tetrapeptide Gly-Pro-Arg-Pro which simulates a moiety of polymerization site E1. The lesser sensitivity of fibrin-desAABB polymerization to the inhibiting tetrapeptide is due to the presence of active site E2 in it. A shape of the concentration dependence curve of the inhibitory effect of tetrapeptide Gly-Pro-Arg-Pro on the polymerization of both fibrin types is similar to the previously found curve for fibrinogen and its fragments--specific inhibitors of polymerization. Ca2+ intensifies inhibition of fibrin-desAABB polymerization by tetrapeptide Gly-Pro-Arg-Pro twice as much as that of fibrin-desAA evidently due to the peptide blockage of sites D2. An increase of the ionic strength from 0.15 to 0.3 enhances the inhibitory effect of the tetrapeptide on polymerization of two monomeric fibrin forms.

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