Hoots W K, Carrell N A, Wagner R H, Cooper H A, McDonagh J
N Engl J Med. 1981 Apr 9;304(15):857-61. doi: 10.1056/NEJM198104093041501.
A 13-year-old girl with chronic aggressive hepatitis, postnecrotic cirrhosis, ulcerative colitis, and a coagulation defect acquired an antibody that specifically interfered with fibrin formation. We sought to characterize the antibody and determine the mechanism of its inhibitory activity. The patient's purified fibrinogen was functionally normal; however, the antibody inhibited the self-assembly of fibrin and prolonged the clotting times of the patient's plasma. This antibody, which belonged to the IgG class of immunoglobulins, acted early in the polymerization process to inhibit the association of fibrin monomers, as indicated by a prolonged lag time and a decreased slope in the polymerization curves. It did not inhibit fibrinopeptide cleavage or fibrin cross-linking. Affinity chromatography indicated that the antibody bound strongly to both fibrinogen and fibrin monomer.
一名患有慢性侵袭性肝炎、坏死后肝硬化、溃疡性结肠炎和凝血缺陷的13岁女孩获得了一种特异性干扰纤维蛋白形成的抗体。我们试图对该抗体进行表征并确定其抑制活性的机制。患者纯化的纤维蛋白原功能正常；然而，该抗体抑制了纤维蛋白的自组装，并延长了患者血浆的凝血时间。这种属于免疫球蛋白IgG类的抗体在聚合过程早期起作用，抑制纤维蛋白单体的缔合，这表现为聚合曲线的延迟时间延长和斜率降低。它不抑制纤维蛋白肽的裂解或纤维蛋白交联。亲和层析表明该抗体与纤维蛋白原和纤维蛋白单体都有很强的结合。
