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

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

Research output: Contribution to journalArticle

1 Scopus citations

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.

Translated title of the contributionInteraction of an analog of the E1 site of tetrapeptide Gly-Pro-Arg-Pro with the D1 site of two forms of monomeric fibrin
Original languageRussian
Pages (from-to)3-9
Number of pages7
JournalUkrainskii biokhimicheskii zhurnal
Volume58
Issue number2
StatePublished - Mar 1 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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