Sereĭskaia A A, Osadchuk T V, Korneliuk A I, Serebrianyĭ S B, Atepalikhina S A
Biokhimiia. 1986 Oct;51(10):1659-66.
It was shown that selective hydrolysis of the disulfide bridge between the A- and B-chains of human thrombin in the absence of denaturating agents decrease its proteolytic (e.g., fibrinogen-binding), esterase and amidase activities. Both chains remain bound by non-covalent interactions. A preparation of partially reduced thrombin was obtained and its kinetic parameters were determined. The experimental results suggest that the S-S bond connecting the A- and B-chains of thrombin is involved in the stabilization of the enzyme active center.
结果表明，在不存在变性剂的情况下，对人凝血酶A链和B链之间的二硫键进行选择性水解会降低其蛋白水解（如纤维蛋白原结合）、酯酶和酰胺酶活性。两条链仍通过非共价相互作用结合在一起。制备了部分还原的凝血酶并测定了其动力学参数。实验结果表明，连接凝血酶A链和B链的S-S键参与了酶活性中心的稳定。
