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

doi:10.1134/S1607672918030067

Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry

Autores: Gorobets M.G.¹, Wasserman L.A.¹, Bychkova A.V.¹, Konstantinova M.L.¹, Plaschina I.G.¹, Rosenfeld M.A.¹
Afiliações:
1. Emanuel Institute of Biochemical Physics
Edição: Volume 480, Nº 1 (2018)
Páginas: 146-148
Seção: 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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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.