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Thromb Haemost 1990; 63(03): 445-448
DOI: 10.1055/s-0038-1645063
Original Article
Schattauer GmbH Stuttgart

Characterization of a Monoclonal Antibody Specific to the Amino Terminus of the α-Chain of Human Fibrin

Simon J T Mao
The Merrell Dow Research Institute, Cincinnati, OH, USA
,
Ann E Rechtin
The Merrell Dow Research Institute, Cincinnati, OH, USA
,
John L Krstenansky
The Merrell Dow Research Institute, Cincinnati, OH, USA
,
Richard L Jackson
The Merrell Dow Research Institute, Cincinnati, OH, USA
› Author Affiliations
Further Information

Publication History

Received 10 August 1989

Accepted after revision 23 February 1990

Publication Date:
30 June 2018 (online)

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Summary

A peptide, Gly-Pro-Arg-Val-Val-Glu, corresponding to the first six residues of the amino terminus of the a-chain of human fibrin (desAA-fihrin) was prepared by solid-phase peptide synthesis. The peptide was covalently linked to keyhole-limpet hemocyanin (KLH) and used as an immunogen for preparing monoclonal antibodies. A monoclonal antibody specific to the hexapeptide, but not to KLH or fibrinogen, was produced. The antibody did not bind to thrombin-mediated clots prepared from either plasma or purified fibrinogen. However, immunoreactivity was detected when fibrin (prepared from fibrinogen) was solubilized with 8 M urea. In contrast, a monoclonal antibody specific to the amino terminus (Gly-His-Arg-Pro-Leu-Asp-Lys) of the (β-chain of fibrin recognized the epitope in clots. These results indicate that thrombin cleavage of fibrinogen produces a structural change in the amino terminal domain of the α-chain that makes it inaccessible to antibody interaction. In addition, our study suggests that the potential clinical application of monoclonal antibodies to localize fibrin-rich thrombi must take into account the final structure of clots.

 

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