Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry. 2018

M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia. maria.g.gorobets@gmail.com.

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.

UI MeSH Term Description Entries
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D011499 Protein Processing, Post-Translational Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility. Amino Acid Modification, Post-Translational,Post-Translational Modification,Post-Translational Protein Modification,Posttranslational Modification,Protein Modification, Post-Translational,Amino Acid Modification, Posttranslational,Post-Translational Amino Acid Modification,Post-Translational Modifications,Post-Translational Protein Processing,Posttranslational Amino Acid Modification,Posttranslational Modifications,Posttranslational Protein Processing,Protein Processing, Post Translational,Protein Processing, Posttranslational,Amino Acid Modification, Post Translational,Modification, Post-Translational,Modification, Post-Translational Protein,Modification, Posttranslational,Modifications, Post-Translational,Modifications, Post-Translational Protein,Modifications, Posttranslational,Post Translational Amino Acid Modification,Post Translational Modification,Post Translational Modifications,Post Translational Protein Modification,Post Translational Protein Processing,Post-Translational Protein Modifications,Processing, Post-Translational Protein,Processing, Posttranslational Protein,Protein Modification, Post Translational,Protein Modifications, Post-Translational
D002152 Calorimetry, Differential Scanning Differential thermal analysis in which the sample compartment of the apparatus is a differential calorimeter, allowing an exact measure of the heat of transition independent of the specific heat, thermal conductivity, and other variables of the sample. Differential Thermal Analysis, Calorimetric,Calorimetric Differential Thermal Analysis,Differential Scanning Calorimetry,Scanning Calorimetry, Differential
D005340 Fibrinogen Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products. Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000072417 Protein Domains Discrete protein structural units that may fold independently of the rest of the protein and have their own functions. Peptide Domain,Protein Domain,Domain, Peptide,Domain, Protein,Domains, Peptide,Domains, Protein,Peptide Domains

Related Publications

M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 2023, Journal of advanced pharmaceutical technology & research,
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 2008, Methods in cell biology,
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 1995, Methods in molecular biology (Clifton, N.J.),
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 1994, Methods in molecular biology (Clifton, N.J.),
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 1974, Methods in enzymology,
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 2002, Methods in molecular biology (Clifton, N.J.),
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
July 1990, Biochemistry,
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
April 2013, Journal of colloid and interface science,
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
November 1999, International journal of biological macromolecules,
M G Gorobets, and L A Wasserman, and A V Bychkova, and M L Konstantinova, and I G Plaschina, and M A Rosenfeld
January 2009, Methods in molecular biology (Clifton, N.J.),
Copied contents to your clipboard!