Antibody-Directed Urokinase: A Specific Fibrinolytic Agent

A specific fibrinolytic agent was synthesized by covalently coupling urokinase to a monoclonal antibody that was fibrin-specific and did not cross-react with fibrinogen. The antibody was raised against a synthetic peptide representing the seven amino-terminal residues of the beta chain of human fibr...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1985-08, Vol.229 (4715), p.765-767
Main Authors: Bode, Christoph, Matsueda, Gary R., Hui, Kwan Y., Haber, Edgar
Format: Article
Language:English
Subjects:
Antibodies
Antibodies, Monoclonal - therapeutic use
Biological and medical sciences
Biotechnology
Cross-Linking Reagents
Drug therapy
Fibrin - immunology
Fibrinolysis
Fibrinolytic agents
Fibrinolytics
Fundamental and applied biological sciences. Psychology
Gels
General pharmacology
Health. Pharmaceutical industry
Heart attack
Humans
In Vitro Techniques
Industrial applications and implications. Economical aspects
Kinetics
man
Medical sciences
Monoclonal antibodies
Other active biomolecules
Pharmaceutical technology. Pharmaceutical industry
Pharmacology. Drug treatments
Physiological aspects
Plasmin
Production of active biomolecules
Radioactive decay
Room temperature
Sodium
Structure-Activity Relationship
Thrombolytic drugs
Thrombosis
Urokinase
Urokinase-Type Plasminogen Activator - administration & dosage
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Description
Summary:A specific fibrinolytic agent was synthesized by covalently coupling urokinase to a monoclonal antibody that was fibrin-specific and did not cross-react with fibrinogen. The antibody was raised against a synthetic peptide representing the seven amino-terminal residues of the beta chain of human fibrin. The urokinaseantifibrin conjugate retained the original binding specificity of the antibody and showed 100-fold increased fibrinolysis in vitro when compared to unmodified urokinase. The presence of human fibrinogen at plasma concentration did not influence these properties.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.4023710