Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry

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详细

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.

作者简介

M. Gorobets

Emanuel Institute of Biochemical Physics

编辑信件的主要联系方式.
Email: maria.g.gorobets@gmail.com
俄罗斯联邦, Moscow, 119334

L. Wasserman

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
俄罗斯联邦, Moscow, 119334

A. Bychkova

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
俄罗斯联邦, Moscow, 119334

M. Konstantinova

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
俄罗斯联邦, Moscow, 119334

I. Plaschina

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
俄罗斯联邦, Moscow, 119334

M. Rosenfeld

Emanuel Institute of Biochemical Physics

Email: maria.g.gorobets@gmail.com
俄罗斯联邦, Moscow, 119334

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