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来自纤维蛋白原Bicêtre II(γ308天冬酰胺→赖氨酸)的凝块的结构与特性。由于孔隙更大、纤维更粗以及刚性降低,导致通透性增加。

Structure and properties of clots from fibrinogen Bicêtre II (gamma 308 Asn-->Lys). Increased permeability due to larger pores, thicker fibers, and decreased rigidity.

作者信息

Marchi R, Loyau S, Anglés-Cano E, Weisel J W

机构信息

Laboratorio de Fisiopatología, Centro de Medicina Experimental, IVIC, Caracas, Venezuela.

出版信息

Ann N Y Acad Sci. 2001;936:125-8.

Abstract

Fibrinogen Bicêtre II is a dysfibrinogenemia in which there is a substitution of Lys for Asn at gamma 308. We have studied the polymerization of this abnormal fibrinogen by measurement of turbidity and have characterized clot structure by scanning electron microscopy, permeation, and viscoelastic measurements. The results of these studies demonstrate that this amino acid substitution has substantial effects on the structure and properties of the clot, resulting in clots made up of thick fibers and large pores with greatly reduced stiffness and increased slippage of protofibrils.

摘要

纤维蛋白原比塞特尔II型是一种异常纤维蛋白原血症,其中γ308位的天冬酰胺被赖氨酸替代。我们通过测量浊度研究了这种异常纤维蛋白原的聚合,并通过扫描电子显微镜、渗透和粘弹性测量对凝块结构进行了表征。这些研究结果表明,这种氨基酸替代对凝块的结构和性质有重大影响,导致凝块由粗纤维和大孔隙组成,硬度大大降低,原纤维的滑动增加。

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