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[纤维蛋白原和纤维蛋白与硫酸鱼精蛋白的相互作用]

[Interaction of fibrinogen and fibrin with protamine sulfate].

作者信息

Mikhalovskaia L I, Varetskaia T V, Belitser V A

出版信息

Ukr Biokhim Zh (1978). 1988 Jul-Aug;60(4):3-9.

PMID:3188253
Abstract

Fibrinogen and fibrin sedimentation by different protamine sulphate preparations have been studied. Ionic strength and protamine sulphate concentration are found to influence the sedimentation reaction (paracoagulation). High sedimentation activity is inherent in protamine sulphate preparations with the lower electrophoretic mobility, that is with the higher molecular weight. The protamine sulphate reaction with fibrinogen and fibrin is of electrostatic character as the long polycationic chain of protamine is coupled with the negatively charged loci either of fibrin or of fibrinogen molecules, thus evoking aggregation. In this case the fibrin molecules being brought together favour the specific mutual binding due to the active sites of polymerization, specific fibres or gel being formed.

摘要

对不同硫酸鱼精蛋白制剂的纤维蛋白原和纤维蛋白沉降情况进行了研究。发现离子强度和硫酸鱼精蛋白浓度会影响沉降反应(副凝集)。具有较低电泳迁移率(即较高分子量)的硫酸鱼精蛋白制剂具有较高的沉降活性。硫酸鱼精蛋白与纤维蛋白原和纤维蛋白的反应具有静电性质,因为鱼精蛋白的长聚阳离子链与纤维蛋白或纤维蛋白原分子的带负电荷位点结合,从而引发聚集。在这种情况下,聚集在一起的纤维蛋白分子由于聚合活性位点而有利于特异性相互结合,形成特定的纤维或凝胶。

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