Effects of dextran on the molecular structure and tensile behaviour of human fibrin.
Characteristic changes induced by dextran during the conversion of fibrinogen to fibrin have previously been shown to be associated with profound alterations in morphology of fibrin. However, whether dextran is incorporated into the fibrin molecule and whether morphological changes are associated with alterations in mechanical behaviour of formed fibrin was unclear. The investigations described show that the fibrin made in the presence of dextran has a shortened syneresis time, a lowered modulus of elasticity, an increased elongation and diminished ultimate strength at break. The molecular composition of fibrin clots remains unaltered despite the altered mechanical properties and morphological changes. Furthermore, dextran is not incorporated into the fibrin structure in any appreciable quantity. It is suggested that these several effects of dextran on clot morphology, tensile behaviour and kinetics of fibrin formation arise from increased forces of attraction between fibrin molecules such that fibrin chains are held together by weak secondary cross-links rather than by stronger primary cross-links which are hidden within the thicker fibrin chain bundles.
D001665:Binding Sites; D003911:Dextrans; D004548:Elasticity; D005337:Fibrin; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism; D006801:Humans; D008968:Molecular Conformation
D003911:Dextrans; D005338:Fibrin Fibrinogen Degradation Products; D005337:Fibrin