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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-08-23
    Description: 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 urokinase-antifibrin 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bode, C -- Matsueda, G R -- Hui, K Y -- Haber, E -- New York, N.Y. -- Science. 1985 Aug 23;229(4715):765-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4023710" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/*therapeutic use ; Cross-Linking Reagents ; Fibrin/immunology ; *Fibrinolysis ; Humans ; In Vitro Techniques ; Kinetics ; Structure-Activity Relationship ; Urokinase-Type Plasminogen Activator/*administration & dosage
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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