Kamykowski G W, Mosher D F, Lorand L, Ferry J D
Biophys Chem. 1981 Feb;13(1):25-8. doi: 10.1016/0301-4622(81)80021-x.
Shear moduli and creep compliances have been measured for four types of clots of human fibrin (about 7 mg/ml) clotted with and without human plasma fibronectin (usually 1.2 mg/ml). Fine clots (with little lateral aggregation of the fibrin protofibrils) were found at pH 8.5, ionic strength 0.45; coarse clots (with substantial lateral aggregation) were formed at pH 7.5, ionic strength 0.15; in both cases with and without ligation by fibrinoligase. In fine clots, the addition of fibronectin without ligation scarcely affected the shear modulus; with ligation, the modulus was decreased by a factor of 0.48. In coarse clots, the shear modulus was increased by addition of fibronectin. The increase was by a factor of 2.0 without ligation and by a factor of 2.4 with ligation. Creep and creep recovery in clots formed with and without fibronectin were similar except for the scale factor represented by the change in modulus.
已对四种类型的人纤维蛋白凝块(约7毫克/毫升)进行了剪切模量和蠕变柔量的测量,这些凝块在添加和不添加人血浆纤连蛋白(通常为1.2毫克/毫升)的情况下凝结而成。在pH 8.5、离子强度0.45时发现了细小凝块(纤维蛋白原纤维的横向聚集很少);在pH 7.5、离子强度0.15时形成了粗大凝块(有大量横向聚集);在这两种情况下均有或没有纤维蛋白连接酶连接。在细小凝块中,未连接时添加纤连蛋白几乎不影响剪切模量;连接时,模量降低了0.48倍。在粗大凝块中,添加纤连蛋白会增加剪切模量。未连接时增加了2.0倍,连接时增加了2.4倍。除了由模量变化表示的比例因子外,添加和不添加纤连蛋白形成的凝块中的蠕变和蠕变恢复情况相似。