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- W2417508769 abstract "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." @default.
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- W2417508769 date "1990-01-01" @default.
- W2417508769 modified "2023-09-26" @default.
- W2417508769 title "Monoclonal Antibodies Specific for a Conformationally Altered State of Fibrinogen" @default.
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- W2417508769 doi "https://doi.org/10.1055/s-0038-1647251" @default.
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