Enzymic activity of thrombin with partially reduced disulfide bonds.
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 beta-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.
D001777:Blood Coagulation; D004220:Disulfides; D006801:Humans; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000378:metabolism*; D014106:Tosylarginine Methyl Ester / Q000378:metabolism
D004220:Disulfides; D014106:Tosylarginine Methyl Ester; D013917:Thrombin