Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry

Dokl Biochem Biophys. 2018 May;480(1):146-148. doi: 10.1134/S1607672918030067. Epub 2018 Jul 14.

Abstract

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.

MeSH terms

  • Calorimetry, Differential Scanning / methods
  • Fibrinogen / chemistry*
  • Humans
  • Oxidation-Reduction
  • Protein Domains
  • Protein Processing, Post-Translational*

Substances

  • Fibrinogen