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纤连蛋白对纤维蛋白凝块剪切模量和蠕变柔量的修饰作用。

Modification of shear modulus and creep compliance of fibrin clots by fibronectin.

作者信息

Kamykowski G W, Mosher D F, Lorand L, Ferry J D

出版信息

Biophys Chem. 1981 Feb;13(1):25-8. doi: 10.1016/0301-4622(81)80021-x.

Abstract

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.

摘要

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。

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