FIGURE 2.

SDS and native PAGE characterization of prelatent antithrombin. Shown are the electrophoretic gels of antithrombin pools A, B, and C (5 μg of protein) obtained during the purification of prelatent antithrombin by Hi-Trap heparin chromatography (Fig. 1) under denaturing (SDS) and native conditions. Native and latent antithrombin samples were run as controls. The ability of each antithrombin (AT) pool to form an SDS-stable complex with a molar excess of thrombin (5 μg) is shown in the SDS gel.