Abstract
The soluble and stable fibrin monomer–fibrinogen complex (SF) is well known to be present in the circulating blood of healthy individuals and of patients with thrombotic diseases. However, its physiological role is not yet fully understood. To deepen our knowledge about this complex, a method for the quantitative analysis of interaction between soluble fibrin monomers and surface‐immobilized fibrinogen has been established by means of resonant mirror (IAsys) and surface plasmon resonance (BIAcore) biosensors. The protocols have been optimized and validated by choosing appropriate immobilization procedures with regeneration steps and suitable fibrin concentrations. The highly specific binding of fibrin monomers to immobilized fibrin(ogen), or vice versa, was characterized by an affinity constant of ∼10^−8^M, which accords better with the direct dissociation of fibrin triads (K~D~ ≈ 10^−8^–10^−9^M) (J. R. Shainoff and B. N. Dardik, Annals of the New York Academy of Science, 1983, Vol. 27, pp. 254–268) than with earlier estimations of the K~D~ for the fibrin–fibrinogen complex (K~D~ ≈ 10^−6^M) (J. L. Usero, C. Izquierdo, F. J. Burguillo, M. G. Roig, A. del Arco, and M. A. Herraez, International Journal of Biochemistry, 1981, Vol. 13, pp. 1191–1196). © 2006 Wiley Periodicals, Inc. Biopolymers 83: 69–82, 2006
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