Jandrot-Perrus M, Aurousseau M H, Rabiet M J, Josso F
Thromb Res. 1982 Sep 15;27(6):659-70. doi: 10.1016/0049-3848(82)90004-4.
In a 81 year old health woman, gross abnormalities of fibrin formation led to the discovery of an abnormal fibrinogen named fibrinogen Bondy. Clottability of purified fibrinogen Bondy was only 53% compared to 95-98% for normal fibrinogen. Functional studies revealed (i) delayed coagulation by thrombin and batroxobin (Reptilase), (ii) incomplete release of fibrino-peptides A and B, (iii) poor fibrin monomer aggregation, (iv) delayed fibrin proteolysis by plasmin. Electrophoretic mobility of fibrinogen Bondy, its three chains and the products of fibrin cross-linking, was normal. Fibrinogen NH2-terminal residues of fibrinogen Bondy were found to be normal. The presence of Ala, in addition to Gly and Tyr in the fibrin clot and its supernatant, showed that a part of fibrinogen molecules was not clotted, i.e. either copolymerised with fibrin or remaining in solutions. Gel filtration of the supernatant allowed the separation of both soluble complexes and fibrinogen. This fibrinogen population was shown to be unclottable by thrombin and to inhibit clotting of normal fibrinogen.
在一位81岁的健康女性中，纤维蛋白形成的明显异常导致发现了一种名为纤维蛋白原邦迪（fibrinogen Bondy）的异常纤维蛋白原。与正常纤维蛋白原的95 - 98%相比，纯化的纤维蛋白原邦迪的凝块形成能力仅为53%。功能研究显示：（i）凝血酶和巴曲酶（立止血）导致凝血延迟；（ii）纤维蛋白肽A和B释放不完全；（iii）纤维蛋白单体聚集不佳；（iv）纤溶酶对纤维蛋白的蛋白水解延迟。纤维蛋白原邦迪及其三条链以及纤维蛋白交联产物的电泳迁移率正常。发现纤维蛋白原邦迪的纤维蛋白原NH2末端残基正常。在纤维蛋白凝块及其上清液中，除了甘氨酸和酪氨酸外还存在丙氨酸，这表明一部分纤维蛋白原分子未形成凝块，即要么与纤维蛋白共聚，要么仍留在溶液中。上清液的凝胶过滤允许分离可溶性复合物和纤维蛋白原。已证明这群纤维蛋白原不能被凝血酶凝结，并能抑制正常纤维蛋白原的凝结。
