Abstract
Partial reduction of thrombin disulfide bridges with dithiothreitol in the absence of denaturants inhibits the fibrinogen clotting but not the esterase activity of the enzyme. The clotting activity reappears on spontaneous air reoxidation of thrombin. As a result of the reaction with dithiothreitol, two disulfide bonds are cleaved in thrombin molecule inducing a small decrease of β-sheets in the secondary structure of thrombin. It may be concluded that this modification does not affect the catalytic site of thrombin but has influence upon the fibrinogen binding (recognition) site.
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