Acyl-enzymes as thrombolytic agents in a rabbit model of venous thrombosis.

Abstract

A derivative of human lys-plasmin in which the active site has been reversibly acylated (BRL 26920; p-anisoyl human lys-plasmin) has been examined as a fibrinolytic agent in a previously described rabbit model of venous thrombosis and shown to be significantly more active and less fibrinogenolytic than free plasmin. A p-anisoylated derivative of a streptokinase (SK)-activated plasmin preparation was significantly less fibrinogenolytic in vivo than the non-acylated enzyme. Acylation increased the fibrinolytic activity of preparations of SK-plasmin activator complexes. BRL 26921, the active site anisoylated derivative of the primary 2-chain SK-plasminogen complex was the most potent fibrinolytic agent studied. SK-Val442-plasminogen complexes, free or acylated, were biologically inactive in this model and confirm the essential nature of fibrin binding processes for effective thrombolysis in vivo.

• Authors: R A Smith, R J Dupe, P D English, J Green
• Journal: Thrombosis and haemostasis (Thromb Haemost) Vol. 47 Issue 3 Pg. 269-74 (Jun 28 1982) ISSN: 0340-6245 [Print] Germany
• PMID: 6214039 (Publication Type: Journal Article)

Chemical References

• Amides
• Fibrin Fibrinogen Degradation Products
• Plasminogen
• Streptokinase
• Fibrinolysin

Topics

• Acylation
• Amides (metabolism)
• Animals
• Fibrin Fibrinogen Degradation Products (metabolism)
• Fibrinolysin (metabolism)
• Fibrinolysis
• Humans
• Plasminogen (metabolism)
• Rabbits
• Streptokinase (pharmacology)
• Thrombophlebitis (drug therapy)