The Fibrinogen-Fibrin Conversion1
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Hydrodynamic characterization of recombinant human fibrinogen species
2013, Thrombosis ResearchHydrodynamic and mass spectrometry analysis of nearly-intact human fibrinogen, chicken fibrinogen, and of a substantially monodisperse human fibrinogen fragment X
2010, Archives of Biochemistry and BiophysicsCitation Excerpt :Considering that the dimensions of the FG species under consideration are at the very limit of detection for angular dependence of the scattered light for the incident wavelength used (658 nm), the Zimm plots in Fig. 10 appear to be rather good. As for 〈[η]〉w, our value for hHMW-FG is ∼9% higher than the “best average” literature value [4,66], but values for bovine FG of 27–30 cm3 g−1 have been also reported [66]. Since the 〈[η]〉w value drops sharply to ∼21 cm3 g−1 for our hFrX preparations, it is conceivable that the accepted 25 cm3 g−1 for unfractionated FG could result from the contribution of species with degraded αC regions, although a 60:40 hHMW-FG:hFrX ratio would be required to achieve that value.
Fibrinogen and fibrin structure and functions
2005, Journal of Thrombosis and HaemostasisCitation Excerpt :Equilateral junctions form with greater frequency when fibrinopeptide cleavage is relatively slow [28], and under such conditions, the networks are more branched and the matrix is ‘tighter’ (i.e. less porous) than those formed at high levels of thrombin [29]. Release of fibrinopeptide B (FPB; Bβ1–14) is slower than release of FPA [11–13]. The process exposes an independent polymerization site, EB [30], beginning with β15–18 gly‐his‐arg‐pro (GHRP) [14] that interacts with a constitutive complementary Db site in the β‐chain segment of the D domain [20,31].
The thrombin-fibrinogen interaction
2004, Biophysical ChemistryInteractions of phospholipid- and poly(ethylene glycol)-modified surfaces with biological systems: Relation to physico-chemical properties and mechanisms
2003, Colloids and Surfaces B: Biointerfaces
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Part of this review was written while one of us (H.A.S.) was at the Carlsberg Laboratorium, Copenhagen, Denmark, as a Fulbright Research Scholar and John Simon Guggenheim Memorial Foundation Fellow.