Jenne D, Hugo F, Bhakdi S
Thromb Res. 1985 May 15;38(4):401-12. doi: 10.1016/0049-3848(85)90138-0.
Complement S-protein is known to function as an inhibitor of the terminal complement sequence (Bhakdi, S. and Tranum-Jensen, J., Biochim. Biophys. Acta 737, 343, 1983). We here report that the S-protein may also play a functional role in haemostasis. Electro-immunoassays performed with the use of poly- and monoclonal antibodies to the protein revealed that it binds to thrombin-anti-thrombin III (T X AT-III) to form stable S X T X AT-III complexes. These complexes form naturally during blood coagulation. They have been identified in human serum and have also been generated in vitro with the respective purified proteins. Formation of the complexes is paralleled by a net protection of thrombin towards the inactivating effects of AT-III, demonstrable in functional assays using a synthetic polypeptide or fibrinogen as substrates for the protease. S-protein may thus exert a promoting effect on blood coagulation and could emerge as a novel component of the blood coagulation system in the future.
已知补体S蛋白可作为末端补体序列的抑制剂（Bhakdi, S.和Tranum-Jensen, J., 《生物化学与生物物理学报》737, 343, 1983）。我们在此报告，S蛋白在止血过程中可能也发挥功能作用。使用针对该蛋白的多克隆和单克隆抗体进行的电免疫测定显示，它与凝血酶 - 抗凝血酶III（T X AT - III）结合形成稳定的S X T X AT - III复合物。这些复合物在血液凝固过程中自然形成。它们已在人血清中被鉴定出来，并且也已通过各自纯化的蛋白质在体外生成。复合物的形成伴随着凝血酶对AT - III失活作用的净保护，这在使用合成多肽或纤维蛋白原作为蛋白酶底物的功能测定中得到证实。因此，S蛋白可能对血液凝固发挥促进作用，并且未来可能成为血液凝固系统的一个新成分。
