[Effect of partial reduction of disulfide bonds on the enzymatic activity of thrombin].
It was demonstrated that partial reduction of disulfide bonds in thrombin by dithiothreitol in the absence of denaturating agents leads to a decrease of enzymatic activity with respect to fibrinogen coagulation and tosylarginine methyl ester hydrolysis. Polyacrylamide gel electrophoresis and determination of the number of SH-groups liberated in the course of reduction suggest that the observed inactivation is primarily due to the disruption of the S-S-bridge between the A- and B-chains of thrombin.
D004220:Disulfides / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013917:Thrombin / Q000378:metabolism* / Q000494:pharmacology; D013918:Thrombin Time
D004220:Disulfides; D013438:Sulfhydryl Compounds; D013917:Thrombin; D004229:Dithiothreitol
Vliianie chastichnogo vosstanovleniia disul'fidnykh sviazeĭ na fermentativnuiu aktivnost' trombina.