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The effect of “aging” of fibrinogen molecule on the structure and properties of fibrin gel

  • Biochemistry
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Abstract

The effect of molecular “aging” of fibrinogen stimulated by preincubation in solution on the fibrin three-dimensional architecture, its ability to crosslink fibrin-stabilizing factor, and the sensitivity of fibringel to plasmin hydrolysis have been studied. The method of elastic light scattering was used to demonstrate that fibrin generated from “defective” fibrinogen had a coarser structure with a higher mean mass-length ratio of polymeric fibers compared to native fibrinogen (2.24 × 109 and 1.46 × 109 g/(mol cm), respectively). Crosslinking had no effect on the architecture of both control and experimental fibrin samples. Spectrophotometric and electrophoretic analysis has shown a higher sensitivity of coarse fibrin gels to plasmin. A close correlation between spontaneous local conformational reconstructions in fibrinogen molecule and its functional activity is concluded.

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Authors and Affiliations

  1. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 119991, Russia

    M. A. Rozenfel’d, V. B. Leonova & M. I. Biryukova

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  1. M. A. Rozenfel’d
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  2. V. B. Leonova
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  3. M. I. Biryukova
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Original Russian Text © M.A. Rozenfel’d, V.B. Leonova, M.I. Biryukova, 2007, published in Izvestiya Akademii Nauk, Seriya Biologicheskaya, 2007, No. 4, pp. 394–401.

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Rozenfel’d, M.A., Leonova, V.B. & Biryukova, M.I. The effect of “aging” of fibrinogen molecule on the structure and properties of fibrin gel. Biol Bull Russ Acad Sci 34, 323–328 (2007). https://doi.org/10.1134/S1062359007040024

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  • DOI: https://doi.org/10.1134/S1062359007040024

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