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Doklady Biochemistry and Biophysics

, Volume 480, Issue 1, pp 146–148 | Cite as

Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry

  • M. G. Gorobets
  • L. A. Wasserman
  • A. V. Bychkova
  • M. L. Konstantinova
  • I. G. Plaschina
  • M. A. Rosenfeld
Biochemistry, Biophysics, and Molecular Biology
  • 25 Downloads

Abstract

For the first time, with the aid of differential scanning calorimetry, the thermal denaturation of fibrinogen under induced oxidation was studied. All fibrinogen structural elements detected by DSC (D region, αC-domain, and E region) are subjected to oxidation. Structural changes in fibrinogen molecule were characterized by the denaturation temperature, denaturation enthalpy, and van’t Hoff enthalpy.

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Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  • M. G. Gorobets
    • 1
  • L. A. Wasserman
    • 1
  • A. V. Bychkova
    • 1
  • M. L. Konstantinova
    • 1
  • I. G. Plaschina
    • 1
  • M. A. Rosenfeld
    • 1
  1. 1.Emanuel Institute of Biochemical PhysicsRussian Academy of SciencesMoscowRussia

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