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- W2020753890 abstract "Tissue-type plasminogen activator (t-PA) has a high affinity for fibrin, which is in contrast to urokinase-type plasminogen activator (u-PA). The relation between the structure and function of t-PA was investigated using monoclonal antibodies and plasmin digested t-PA fragments. The results obtained indicated that the three dimensional structure of kringle 2 is necessary for t-PA to develop its fibrin affinity. The monoclonal antibodies which interfered with the fibrin binding ability of native t-PA had two separate epitopes, one in kringle 2 and other in the N-terminal region of the light chain of t-PA." @default.
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- W2020753890 date "1988-09-01" @default.
- W2020753890 modified "2023-10-17" @default.
- W2020753890 title "Monoclonal antibody interferes with fibrin binding of t-PA" @default.
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- W2020753890 doi "https://doi.org/10.1016/0049-3848(88)90114-4" @default.
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