Monoclonal antibodies specific for a conformationally altered state of fibrinogen.
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 soluble 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.
Zamarron
C
C
Research Institute of Scripps Clinic, La Jolla, California 92037.
Ginsberg
M H
MH
Plow
E F
EF
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000302:isolation & purification; D000918:Antibody Specificity / Q000276:immunology; D001704:Biopolymers; D000939:Epitopes / Q000032:analysis; D005337:Fibrin / Q000096:biosynthesis; D005340:Fibrinogen / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D007118:Immunoassay; D015151:Immunoblotting; D051379:Mice; D008807:Mice, Inbred BALB C; D011487:Protein Conformation; D012995:Solubility; D013499:Surface Properties
D000911:Antibodies, Monoclonal; D001704:Biopolymers; D000939:Epitopes; D005337:Fibrin; D005340:Fibrinogen