[HTML][HTML] Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor∗
L Bajzar, R Manuel, ME Nesheim - Journal of Biological Chemistry, 1995 - ASBMB
Previous studies demonstrated that tissue plasminogen activator-induced fibrinolysis in vitro
is retarded in the presence of prothrombin (II) activation and that the anticoagulant-activated
protein C appears profibrinolytic by preventing the formation of thrombin (IIa)-like activity
during fibrinolysis. To disclose the molecular connection between the generation of IIa and
the inhibition of fibrinolysis, a lysis assay that is sensitive to the antifibrinolytic effect of II
activation was developed and was used to purify a 60-kDa single-chain protein from human …
is retarded in the presence of prothrombin (II) activation and that the anticoagulant-activated
protein C appears profibrinolytic by preventing the formation of thrombin (IIa)-like activity
during fibrinolysis. To disclose the molecular connection between the generation of IIa and
the inhibition of fibrinolysis, a lysis assay that is sensitive to the antifibrinolytic effect of II
activation was developed and was used to purify a 60-kDa single-chain protein from human …