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.
Kazama
M
M
Department of Medicine, School of Medicine, Teikyo University, Tokyo, Japan.
Tahara
C
C
Abe
T
T
Kasai
K
K
D001120:Arginine; D002846:Chromatography, Affinity; D005337:Fibrin / Q000378:metabolism*; D008239:Lysine; D010446:Peptide Fragments / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism; D010959:Tissue Plasminogen Activator / Q000378:metabolism; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism
D010446:Peptide Fragments; C018998:lysyl-plasminogen; D005337:Fibrin; D010958:Plasminogen; D001120:Arginine; D010959:Tissue Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator; D008239:Lysine