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Thromb Haemost 1990; 64(01): 041-046
DOI: 10.1055/s-0038-1647251
Original Article
Schattauer GmbH Stuttgart

Monoclonal Antibodies Specific for a Conformationally Altered State of Fibrinogen[*]

Concepcion Zamarron
The Committee on Vascular Biology, Research lnstitute of Scripps Clinic, La Jolla, California, USA
,
Mark H Ginsberg
The Committee on Vascular Biology, Research lnstitute of Scripps Clinic, La Jolla, California, USA
,
Edward F Plow
The Committee on Vascular Biology, Research lnstitute of Scripps Clinic, La Jolla, California, USA
› Author Affiliations
Further Information

Publication History

Received 10 January 1990

Accepted after revision 14 May 1990

Publication Date:
25 July 2018 (online)

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Summary

Four monoclonal antibodies were selected by their ability to discriminate surface-bound from soluble fibrinogen. These antibodies reacted with insolubilized fibrinogen but not other immobilized proteins and their reaction with surface-bound fibrinogen was not diminished by a 100-fold excess of sotuble fibrinogen. The antibodies reacted with the same or spatially proximal epitopes, and the recognized epitope(s) resided within the gamma chain segment of the D domain of fibrinogen. Fab fragments of the antibodies inhibited fibrin polymerization in a dose dependent manner, suggesting that the epitope(s) was also exposed by the conversion of fibrinogen to fibrin. These data indicate that adsorption of fibrinogen onto a surface induces conformational changes and that similar changes are also evoked when fibrinogen is converted into fibrin.

Dedicated to Professor M. Verstraete on the occasion of his 65th birthday


 

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