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The Development of Radioimmunoassays for Fibrinogen Degradation Products: Fragments D and E
Author(s) -
Gordon Y. B.,
Martin M. J.,
Landon J.,
Chard T.
Publication year - 1975
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1975.tb01804.x
Subject(s) - radioimmunoassay , fibrinogen , chemistry , chromatography , plasmin , antibody , degradation (telecommunications) , microbiology and biotechnology , biochemistry , biology , immunology , enzyme , computer science , telecommunications
S ummary . Fibrinogen degradation products, fragment D (FgD) and fragment E (FgE) have been measured in human serum by specific radioimmunoassays. In addition, the appearance of a neoantigenic determinant on FgD, revealed when fibrinogen is degraded by plasmin has been utilized to develop a specific radioimmunoassay for FgD in plasma (FgD neo ). The reagents and conditions used in each assay are described in detail. The mean specific activity was 144 μCi/μg for 125 I‐labelled FgE and 82 μCi/μg for 125 I‐labelled FgD. Separation of antibody bound and free antigen was achieved using second antibody. The detection limits of the FgE, FgD and FgD neo assays were 0.8, 1.0 and 6.2 ng/ml respectively. The specificity of each assay with respect to fibrinogen and its degradation fragments has been assessed. Fibrinogen and fragment X cross‐reacted markedly in both the FgE and FgD assays, whereas the cross‐reaction of fibrinogen was abolished in the FgD neo assay, while the cross‐reaction of fragment X was 10%, indicating gradual emergence of the neoantigenic site during digestion of fibrinogen. The sensitivity, precision, and specificity of the radioimmunoassay systems described have major advantages over the existing procedures for the measurement of fibrinogen degradation products.