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Self-assembly of soluble unlinked and cross-linked fibrin oligomers

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Abstract

Self-assembly of soluble unlinked and cross-linked fibrin oligomers formed from desA-fibrin monomer under the influence of factor XIIIa was studied in the presence of non-denaturing urea concentrations. By methods of elastic and dynamic light scattering combined with analytical ultracentrifugation, desA-fibrin oligomers formed in both the presence and absence of the factor XIIIa were shown to be ensembles consisting of soluble rod-like double-stranded protofibrils with diverse weight and size. Unlinked and cross-linked soluble double-stranded protofibrils can reach the length of 350–450 nm. The structure of soluble covalently-linked protofibrils is stabilized by isopeptide γ-dimers. Electrophoretic data indicate a complete absence of isopeptide bonds between α-chains of desA-fibrin molecules. The molecular mechanism of formation of soluble rod-like fibrin structures and specific features of its covalent stabilization under the influence of factor XIIIa are discussed.

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Authors and Affiliations

  1. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, 119334, Moscow, Russia

    M. A. Rosenfeld, V. B. Leonova, M. I. Biryukova & M. V. Vasileva

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  1. M. A. Rosenfeld
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  2. V. B. Leonova
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  3. M. I. Biryukova
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  4. M. V. Vasileva
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Correspondence to M. A. Rosenfeld.

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Original Russian Text © M. A. Rosenfeld, V. B. Leonova, M. I. Biryukova, M. V. Vasileva, 2011, published in Biokhimiya, 2011, Vol. 76, No. 10, pp. 1416–1427.

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Rosenfeld, M.A., Leonova, V.B., Biryukova, M.I. et al. Self-assembly of soluble unlinked and cross-linked fibrin oligomers. Biochemistry Moscow 76, 1155–1163 (2011). https://doi.org/10.1134/S0006297911100099

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  • DOI: https://doi.org/10.1134/S0006297911100099

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