An investigation of the physical status of fibrinogen that has been adsorbed to glass and then eluted has been conducted. Exposure of Kabi fibrinogen to glass was carried out using a glass bead column experiment. The fibrinogen was eluted sequentially, first by 1 M Tris and then by SDS. The initially eluted fibrinogen showed considerable degradation (SDS polyacrylamide gel electrophoresis) while the later fractions were less degraded. Fibrinogen purified by chromatography on either DEAE-cellulose or Sepharose-lysine to remove plasminogen was less degraded. When purified plasminogen was added to fibrinogen, degradation of column eluates was very extensive in all eluted fractions. These results are interpreted in terms of a surface-mediated activation of plasminogen to plasmin followed by fibrinogenolysis. Although such an effect remains to be demonstrated as a general property of surfaces, it is speculated that surfaces may vary in their activation of fibrinolysis as well as their activation of clotting, and that maximization of fibrinolysis is a worthwhile goal in the development of blood-compatible surfaces.