title: [Fibrinolytic activity of acyl-urokinase].
abstract: Urokinase was acylated at the active site serine hydroxyl using p-amidinophenyl benzoate or p-nitrophenyl p'-guanidinobenzoate. The enzymatically inactive acyl-urokinase was reactivated in buffer (pH 7.5) or plasma at 37 degrees C with a half-life of 11 min (benzoyl-urokinase) or 10 h (p-guanidinobenzoyl-urokinase). Upon administration (50,000 IU/kg) to rabbits, urokinase was more rapidly eliminated than either acyl-enzyme. The results suggest that urokinase is eliminated via the binding to plasma inhibitors.
mesh_terms: D000215:Acylation; D000818:Animals; D001550:Benzamidines; D001565:Benzoates; D001665:Binding Sites; D005340:Fibrinogen / Q000378:metabolism; D005342:Fibrinolysis; D006801:Humans; D007700:Kinetics; D011817:Rabbits; D012694:Serine; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
chemical_list: D001550:Benzamidines; D001565:Benzoates; C002238:4-nitrophenyl 4'-guanidinobenzoate; D012694:Serine; C006491:4-amidinophenylbenzoate; D005340:Fibrinogen; D014568:Urokinase-Type Plasminogen Activator
vernacular_title: Untersuchungen zur fibrinolytischen Aktivität von Acyl-Urokinase.