:Effects on activated protein C and its zymogen

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Thirteen monoclonal antibodies to human protein C were prepared according to the hybridoma technique of Köhler and Milstein using BALB/c mice and murine myeloma cells (P3Ul). The antibodies were characterized where they recognize on the protein C molecule and whether they effect on the biological functions of protein C. Immunoblotting technique clarified that six antibodies bound to the L-chain of protein C and five antibodies to the H-chain. Two antibodies neither bound to the L-chain nor the H-chain, though they bound to the nonreduced protein C. Two of the antibodies directing toward the H-chain (MFC-1, 13) inhibited the amidolytic activity of activated protein C. In addition to these two, another one toward the H-chain (MFC-10) and two toward the L-chain (MFC-9, 11) inhibited the Factor Va inactivation of activated protein C. One of the antibodies which inhibited the amidolytic activity of the enzyme (MFC-1) blocked the inhibition of the enzyme by protein C inhibitor. Another one toward the H-chain (MFC-5) inhibited the activation of protein C by thrombin regardless of the presence or absence of thrombomodulin. These results would further inform us the relationship between the structure and function of protein C.
一般社団法人日本血栓止血学会の論文