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Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry


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Resumo

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.

Sobre autores

M. Gorobets

Emanuel Institute of Biochemical Physics

Autor responsável pela correspondência
Email: maria.g.gorobets@gmail.com
Rússia, Moscow, 119334

L. Wasserman

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
Rússia, Moscow, 119334

A. Bychkova

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
Rússia, Moscow, 119334

M. Konstantinova

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
Rússia, Moscow, 119334

I. Plaschina

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
Rússia, Moscow, 119334

M. Rosenfeld

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
Rússia, Moscow, 119334

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Declaração de direitos autorais © Pleiades Publishing, Ltd., 2018