Shigekiyo T, Kosaka M, Shintani Y, Azuma H, Iishi Y, Saito S
First Department of Internal Medicine, School of Medicine, University of Tokushima, Japan.
Acta Haematol. 1989;81(3):160-5. doi: 10.1159/000205551.
The mechanism of inhibition of fibrin monomer polymerization was studied in a patient with primary amyloidosis. Thrombin and reptilase times of the patient's purified fibrinogen (Fbg) were remarkably prolonged, and polymerization of the patient's fibrin monomer was disturbed. Fbg-Bence Jones protein (BJP) complex was demonstrated by immunoelectrophoresis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis on the patient's purified Fbg. The patient's BJP not only prolonged the thrombin time of normal Fbg but also inhibited the polymerization of normal fibrin monomer. These results suggested that in this patient fibrin monomer polymerization was inhibited by binding of BJP to Fbg.
对一名原发性淀粉样变性患者抑制纤维蛋白单体聚合的机制进行了研究。该患者纯化纤维蛋白原（Fbg）的凝血酶时间和蛇毒凝血酶时间显著延长，其纤维蛋白单体的聚合受到干扰。通过免疫电泳和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳在该患者的纯化Fbg上证实了Fbg-本斯·琼斯蛋白（BJP）复合物。该患者的BJP不仅延长了正常Fbg的凝血酶时间，还抑制了正常纤维蛋白单体的聚合。这些结果表明，在该患者中，BJP与Fbg结合抑制了纤维蛋白单体的聚合。
