Sereĭskaia A A, Osadchuk T V, Serebriannyĭ S B
Biokhimiia. 1985 Aug;50(8):1278-83.
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.
已证明，在不存在变性剂的情况下，用二硫苏糖醇对凝血酶中的二硫键进行部分还原会导致其对纤维蛋白原凝固和甲苯磺酰精氨酸甲酯水解的酶活性降低。聚丙烯酰胺凝胶电泳以及对还原过程中释放的SH基团数量的测定表明，观察到的失活主要是由于凝血酶A链和B链之间的S-S桥被破坏。
