Interaction of heparin with fibronectin and isolated fibronectin domains

摘要: Fluorescence polarization, gel exclusion chromatography and affinity were used to characterize the interaction of heparins different size with human plasma fibronectin (Fn) several its isolated domains. The fluid-phase Fn heparin was dominated by 30 kDa 40 Hep-2 domains located near C-terminal ends A B chains respectively. Hep-2A domain from heavy chain indistinguishable Hep-2B in this respect; presence an additional type III homology unit latter had no effect on binding. Evidence provided that each has two binding sites for heparin. N-terminal Hep-1 reacted weakly fluid phase even though it binds strongly immobilized fragments rather undiscriminating their reaction fluoresceinamine-labelled sizes. However, oligosaccharides smaller than tetradecasaccharide (14-mer) bound a 5-10-fold lower affinity. These results suggest are able recognize broad spectrum presumably vary significantly respect amount spatial distribution charge.