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Antibodies to the β‐amyloid peptide cross‐react with conformational epitopes in human fibrinogen subunits from peripheral blood
Author(s) -
Stem Robert A.,
Trojanowski John Q.,
Lee Virginia M.-Y.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80760-g
Subject(s) - fibrinogen , antibody , epitope , antiserum , chemistry , fibrin , peptide , biochemistry , amyloid (mycology) , microbiology and biotechnology , immunology , biology , inorganic chemistry
Antibodies to the Alzheimer disease (AD) β‐amyloid peptide (βAP) were used to identify βAP precursor fragments in blood. The antibodies detected 3 major polypeptides with apparent molecular weights (MW) of 47‐64000 in Western blots of plasma derived clot proteins, but these proteins corresponded to human A‐α, B‐β and γ‐fibrinogen since they reacted with 2 different anti‐fibrinogen antisera, and the anti‐βAP and anti‐fibrinogen antibodies recognized purified fibrinogen and fibrin. These data are significant for efforts to develop immunochemical assays to diagnose and monitor the progression of AD.