Thromb Haemost 1987; 57(01): 082-086
DOI: 10.1055/s-0038-1651067
Original Articles
Schattauer GmbH Stuttgart

Mapping of Epitopes on Human Tissue-Type Plasminogen Activator with Recombinant Deletion Mutant Proteins

Anton-Jan van Zonneveld
The Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Depts. of Molecular Biology and Autoimmune Diseases, Amsterdam, The Netherlands
,
Harry Veerman
The Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Depts. of Molecular Biology and Autoimmune Diseases, Amsterdam, The Netherlands
,
Just P J Brakenhoff
The Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Depts. of Molecular Biology and Autoimmune Diseases, Amsterdam, The Netherlands
,
Lucien A Aarden
The Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Depts. of Molecular Biology and Autoimmune Diseases, Amsterdam, The Netherlands
,
Jean-Francois Cajot
*   The Swiss Institute for Experimental Cancer Research, Epalinges, Switzerland
,
Hans Pannekoek
The Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Depts. of Molecular Biology and Autoimmune Diseases, Amsterdam, The Netherlands
› Author Affiliations
Further Information

Publication History

Received 22 August 1986

Accepted after revision 25 November 1986

Publication Date:
06 July 2018 (online)

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Summary

An antigen assay based on a monoclonal antibody directed against the light chain of tissue-type plasminogen activator (t-PA) was developed to quantify seven recombinant (r) t-PA deletion mutant proteins. These recombinant proteins were then employed to map different epitopes on t-PA which interact with a panel of twenty-three monoclonal anti-t-PA antibodies. Twenty were directed against domains on the heavy chain, two against the “finger” domain, three against the “epidermal growth factor-like” domain, five against the kringle 1 domain, and ten against the kringle 2 domain. Only three monoclonal anti-t-PA antibodies interact with the light chain. The finding that the epitopes of each of the monoclonals could be determined with the deletion mutant proteins supports the hypothesis of autonomous folding of structural domains and emphasizes the validity of the use of the recombinant t-PA-deletion mutant proteins for structure-function studies.