Email this article Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry
- Authors: Gorobets M.G.1, Wasserman L.A.1, Bychkova A.V.1, Konstantinova M.L.1, Plaschina I.G.1, Rosenfeld M.A.1
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Affiliations:
- Emanuel Institute of Biochemical Physics
- Issue: Vol 480, No 1 (2018)
- Pages: 146-148
- Section: Biochemistry, Biophysics, and Molecular Biology
- URL: https://journals.rcsi.science/1607-6729/article/view/212275
- DOI: https://doi.org/10.1134/S1607672918030067
- ID: 212275
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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.
About the authors
M. G. Gorobets
Emanuel Institute of Biochemical Physics
Author for correspondence.
Email: maria.g.gorobets@gmail.com
Russian Federation, Moscow, 119334
L. A. Wasserman
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Russian Federation, Moscow, 119334
A. V. Bychkova
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Russian Federation, Moscow, 119334
M. L. Konstantinova
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Russian Federation, Moscow, 119334
I. G. Plaschina
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Russian Federation, Moscow, 119334
M. A. Rosenfeld
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Russian Federation, Moscow, 119334
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