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© Institut Pasteur
Structure de macromolécules : dimère d'aquométhémoglobine de cheval. Dérivé toxique oxydé de l'hémoglobine, représentant 1 à 2% du total.
Publication : Thrombosis research

Hydrodynamic characterization of recombinant human fibrinogen species

Team: Molecular Biophysics
Member: Patrick England
Member: Bertrand Raynal
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Thrombosis research - 30 Apr 2013

Raynal B, Cardinali B, Grimbergen J, Profumo A, Lord ST, England P, Rocco M

Link to Pubmed [PMID] – 23642654

Thromb. Res. 2013 Jul;132(1):e48-53

Fibrinogen is a key component of the blood coagulation system and plays important, diverse roles in several relevant pathologies such as thrombosis, hemorrhage, and cancer. It is a large glycoprotein whose three-dimensional molecular structure is not fully known. Furthermore, circulating fibrinogen is highly heterogeneous, mainly due to proteolytic degradation and alternative mRNA processing. Recombinant production of human fibrinogen allows investigating the impact on the three-dimensional structure of specific changes in the primary structure.