Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry
- Авторы: 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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Учреждения:
- Emanuel Institute of Biochemical Physics
- Выпуск: Том 480, № 1 (2018)
- Страницы: 146-148
- Раздел: 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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Аннотация
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.
Об авторах
M. Gorobets
Emanuel Institute of Biochemical Physics
Автор, ответственный за переписку.
Email: maria.g.gorobets@gmail.com
Россия, Moscow, 119334
L. Wasserman
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Россия, Moscow, 119334
A. Bychkova
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Россия, Moscow, 119334
M. Konstantinova
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Россия, Moscow, 119334
I. Plaschina
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Россия, Moscow, 119334
M. Rosenfeld
Emanuel Institute of Biochemical Physics
Email: maria.g.gorobets@gmail.com
Россия, Moscow, 119334
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