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Monoclonal antibodies directed against human alpha thrombin ec 3.4.21.5 and the thrombin antithrombin iii complex


Monoclonal antibodies directed against human alpha thrombin ec 3.4.21.5 and the thrombin antithrombin iii complex



Thrombosis Research 36(5): 397-410



ISSN/ISBN: 0049-3848

Human .alpha.-thrombin was poorly immunogenic in Balb/c mice. Following fusion of spleen cells from a responding mouse with NS-1 cells, 8 mouse monoclonal antibodies against .alpha.-thrombin were isolated, and 6 were characterized. Five of these were isotype IgG2a, and 1 was IgG1. One, EST 1, bound thrombin only minimally, and was directed against a neoantigen on the thrombin-ATIII (T-AT) complex. This antibody also recognized a site on prothrombin, though with much lower affinity. Its binding was markedly temperature-dependent, indicating a requirement for molecular mobility. A 2nd antibody, EST 4, would not bind the T-AT complex. It inhibited both the clotting and amidase activities of thrombin, and modification of the active site histidine, but not the active site serine, reduced the affinity constant of binding to EST 4. This antibody appears to be directed against an epitope in the vicinity of the enzyme active site. The epitopes for EST 1 and EST 4 were both remote from those of the other monoclonal antibodies, EST 2, 6, 7 and 8. These 4 competed with each other for binding to thrombin, and all inhibited clotting but not amidase activity. Thrombin binding was not affected by modification of the active site, though formation of the T-AT complex reduced the affinity of binding to EST 6 and EST 8. These monoclonals recognize epitopes in the region of the fibrinogen binding site.

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Accession: 005923610

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