Quantitative analysis of fibrin-binding affinity of fibrinolytic components by frontal affinity chromatography.

Binding affinity of fibrinolytic factors to insolubilized lysine and fibrin was quantitatively measured by frontal affinity chromatography using lysine-Toyopearl and fibrin-Sepharose column. The highest binding affinity was found with recombinant tissue-type plasminogen activator (t-PA), followed by lysyl-plasminogen and glutamyl-plasminogen (Glu-PLg) with intermediate affinity, but very low affinity by single chain UK-type plasminogen activator, high molecular weight UK and low molecular weight UK. At the coexistence of EACA, fibrin-binding affinity of Glu-PLg was greatly reduced, but those of UK's were substantially unchanged. It was concluded that high fibrin-binding affinity of t-PA and plasminogens were largely related to the lysine-binding affinity of these enzymes, but that of UK's would be related to the other binding affinity.