Artikkelens første del viser hvordan FN blir representert på to forskjellige måter i norsk utenrikspolitisk debatt: den ene side pragmatisk, som legitimeringsarena for ført politikk, og annen ideologisk, alternativ til Nato-orientert politikk. Spenningen mellom de kommer tydelig frem idet begrepet «FN-sporet» ble vanlig ordskifte omkring Irak-krigen (2003), umiddelbart brukt begge måter. Del at...

Different fibronectin (FN) isoforms arise via alternate splicing of a single gene transcript in a cell- and tissue-specific manner. Antibodies were used to evaluate the presence and distribution of FN and its isoforms in Dupuytren's diseased and normal palmar fascia. Immunolocalization studies show extracellular FN fibrils, including FN isoforms containing extra domains A (A-FN) and B (B-FN), i...

Large quantities of fibronectin (Fn) are present in inflammatory synovial fluid. Inflammatory synovial fluid Fn, while indistinguishable from plasma Fn on the basis of reactivity to polyclonal antibodies, displays alterations in molecular size and charge. Since biochemical differences between plasma and synovial fluid fibronectins might be in part due to differences in glycosylation we have com...

(1-2) F<„'> £ FWFi , 1=0 However, there are some easier methods of calculation. Let the Fibonacci polynomials Fn(x) be defined by (1.3) Fn+2(x) = xFn+1(x) + Fn(x), Fo(x)~0, F7(x) = 1 . Then, since Fn(1)= Fn, the recursion relation for the Fibonacci numbers, Fn+2= Fn+i + Fn, follows immediately by taking x = I In a similar manner we may write recursion relations for {Fff^} . From (1.3), taking t...

We have investigated the interactions between plasma fibronectin (Fn) and human peripheral blood phagocytic cells. As shown by studies of the binding of Fn-coated fluorescent microspheres (Fn-ms), both polymorphonuclear leukocytes (PMN) and monocytes had specific binding sites for Fn at the plasma membrane. However, as purified from blood, only monocytes were stimulated by Fn to become more act...

Fluorescence resonance energy transfer (FRET) between fluorophores attached to single proteins provides a tool to study the conformation of proteins in solution and in cell culture. As a protein unfolds, nanometer-scale increases in distance between donor and acceptor fluorophores cause decreases in FRET. Here we demonstrate the application of FRET to imaging coexisting conformations of fibrone...