ArticleThrombosis research2013
Hydrodynamic characterization of recombinant human fibrinogen species.
Article in Thrombosis research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026Review
- Protein translational diffusion as a way to detect intermolecular interactions.Biophysical reviews · 2023Review
- Fibrinogen αC-regions are not directly involved in fibrin polymerization as evidenced by a "Double-Detroit" recombinant fibrinogen mutant and knobs-mimic peptides.Journal of thrombosis and haemostasis : JTH · 2020Article
- Atomic Structural Models of Fibrin Oligomers.Structure (London, England : 1993) · 2018Article
- Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization.Nanoscale · 2017Article
- Fibrin Formation, Structure and Properties.Sub-cellular biochemistry · 2017Review
- Fibrinogen species as resolved by HPLC-SAXS data processing within theJournal of applied crystallography · 2013Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
introductionFibrinogen 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.
methodsWe performed analytical ultracentrifugation analyses of a full-length recombinant human fibrinogen, its counterpart purified from human plasma, and a recombinant human fibrinogen with both Aα chains truncated at amino acid 251, thus missing their last 359 amino acid residues.
resultsWe have accurately determined the translational diffusion and sedimentation coefficients (Dt(20,w)(0), s(20,w)(0)) of all three species. This was confirmed by derived molecular weights within 1% for the full length species, and 5% for the truncated species, as assessed by comparison with SDS-PAGE/Western blot analyses and primary structure data. No significant differences in the values of Dt(20,w)(0) and s(20,w)(0) were found between the recombinant and purified full length human fibrinogens, while slightly lower and higher values, respectively, resulted for the recombinant truncated human fibrinogen compared to a previously characterized purified human fibrinogen fragment X obtained by plasmin digestion.
conclusionsFull-length recombinant fibrinogen is less polydisperse but hydrodynamically indistinguishable from its counterpart purified from human plasma. Recombinant Aα251-truncated human fibrinogen instead behaves differently from fragment X, suggesting a role for the Bβ residues 1-52 in inter-molecular interactions. Overall, these new hydrodynamic data will constitute a reliable benchmark against which models of fibrinogen species could be compared.
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