Abstract
It is of great interest to know whether proteins adsorbed on a solid surface are conformationally altered, particularly for the problem of blood-foreign surface interaction. With this aim in mind, we tested the reactivities of immobilized or soluble fibrinogen against monoclonal antibodies obtained by mouse immunization with fibrin derivatives. Using an immunoenzymological assay with a monoclonal antibody that revealed an epitope present in the D domain of the molecule but not exposed on soluble undegraded fibrinogen, we found that the binding of fibrinogen to polystyrene rendered the epitope accessible to the monoclonal antibody. We speculate with these results that a conformational alteration of fibrinogen occurred by adsorption to the solid phase. Such results may have important applications in the testing of artificial surfaces that are designed to come in contact with the circulation.
Published Version
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