利用差示扫描量热法研究人纤维蛋白原的氧化修饰
Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry.
作者信息
Gorobets M G, Wasserman L A, Bychkova A V, Konstantinova M L, Plaschina I G, Rosenfeld M A
机构信息
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia.
出版信息
Dokl Biochem Biophys. 2018 May;480(1):146-148. doi: 10.1134/S1607672918030067. Epub 2018 Jul 14.
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.
首次借助差示扫描量热法研究了诱导氧化下纤维蛋白原的热变性。差示扫描量热法检测到的所有纤维蛋白原结构元件（D区、αC结构域和E区）都受到氧化作用。纤维蛋白原分子的结构变化通过变性温度、变性焓和范特霍夫焓来表征。
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