Jan E. Dyr,1 Marketa Jirouskova,1 Jitka Rysava,1 Ivo Tichy,2 Petr Tobiska,2 Radan Slavik,2 Jiri Homola,3 Jiri Suttnar1
1Institute of Hematology and Blood Transfusion (Czech Republic) 2Institute of Radio Engineering and Electronics (Czech Republic) 3Institute of Radio Engineering and Electronics (United States)
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The exploitation of surface plasmon resonance optical sensor for the study of the interaction of immobilized fibrinogen and fibrin monomer with soluble fibrinogen and thrombin is reported. Soluble fibrinogen was mostly reversible, the bound thrombin could be inhibited by milimolar concentration of phenylmethylsulphonyl fluoride (PMSF). At lease three sets of different thrombin binding sites were found. There was a residual fraction of thrombin bound to washed fibrin (ogin) (to about a five to ten percent of fibron monomer units) suggesting that a known naturally occurring fibrinogen variant differing in the gamma chain was the target. Surface bound fibrinogen was converted by thrombin to fibrin monomer that interacted with fibrinogen in solution. At low fibrin monomer surface density the second layer was formed that contained about the same amount of protein as the first layer, at higher fibrin monomer concentration less than one molecule of fibrinogen per molecule of fibrin monomer was captured. Starting with surface-bound fibrinogen and alternating addition of thrombin and fibrinogen a fibrin network of predetermined composition, size, and arrangement could be formed.
Jan E. Dyr,Marketa Jirouskova,Jitka Rysava,Ivo Tichy,Petr Tobiska,Radan Slavik,Jiri Homola, andJiri Suttnar
"Surface plasmon resonance analysis of immobilized fibrinogen and fibrin and their interaction with thrombin and fibrinogen", Proc. SPIE 3570, Biomedical Sensors, Fibers, and Optical Delivery Systems, (15 January 1999); https://doi.org/10.1117/12.336928
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Jan E. Dyr, Marketa Jirouskova, Jitka Rysava, Ivo Tichy, Petr Tobiska, Radan Slavik, Jiri Homola, Jiri Suttnar, "Surface plasmon resonance analysis of immobilized fibrinogen and fibrin and their interaction with thrombin and fibrinogen," Proc. SPIE 3570, Biomedical Sensors, Fibers, and Optical Delivery Systems, (15 January 1999); https://doi.org/10.1117/12.336928