Sereĭskaia A A, Kostiuchenko N V, Osadchuk T V, Serebrianyĭ S B
Ukr Biokhim Zh (1978). 1983;55(3):277-80.
Partial dithiothreitol-reduction of the disulphide thrombin bonds when denaturating agents are absent lowers significantly enzymic activity of thrombin relative to fibrinogen coagulation. This permits supposing that at least one of the disulphide bridges in a thrombin molecule is necessary for stabilization of the space structure important for a specific hydrolysis of fibrinogen.
在不存在变性剂的情况下，对凝血酶的二硫键进行部分二硫苏糖醇还原，会显著降低凝血酶相对于纤维蛋白原凝血的酶活性。由此可以推测，凝血酶分子中的至少一个二硫键对于稳定对纤维蛋白原特异性水解至关重要的空间结构是必要的。
