Abstract
Thrombin adsorbed onto Cuprophane or poly(vinyl chloride) (PVC) was shown to be inactive with respect to amidase activity. Desorbed thrombin from these two artificial surfaces showed only low amidase activity. However, in the presence of albumin, the surfaceβbound thrombin appeared to exhibit increased amidase activity. This apparent activity may be due to the action of thrombin displaced from the surfaces by albumin. Thrombin bound to Cuprophane or PVC was shown to be capable of reacting with antithrombin III (AT III) only in the presence of heparin. On the other hand, AT III bound to Cuprophane or PVC was unable to react with thrombin in either the absence or presence of heparin. Fibrin formation on or at surfaces was demonstrated by phase contrast microscopy when Cuprophane or PVC pretreated with thrombin and carefully rinsed was incubated in a fibrinogen solution. This fibrin formation is time dependent and likely is the result of direct interaction of adsorbed thrombin with fibrinogen in solution. Glass, Cuprophane, and PVC pretreated with thrombin were shown to attract more platelets than respective untreated surfaces. The enhancing effect of adsorbed thrombin on platelet adhesion was similar to the enhancing effect of adsorbed fibrinogen. Thrombin adsorbed onto PVC and crosslinked by glutaraldehyde treatment was shown to be antigenically active with a ^125^Iβlabeled monospecific antithrombin IgG produced in rabbits. No other plasma proteins adsorbed singly or from plasma or serum onto PVC reacted significantly with the antithrombin IgG preparation. The possible significance of these observations is discussed.