鱼精蛋白与纤维蛋白原的d结构域相互作用

Kazunori Okano, Yuji Saito, Ayako Matsushima, Yuji Inada
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引用次数: 13

摘要

纤维蛋白原在一种碱性蛋白,鱼精蛋白存在下沉淀的机制已经被研究过。d片段的加入对沉淀有明显的抑制作用。纤维蛋白原的光氧化消除了凝血酶引起的结合力,但对鱼精蛋白引起的沉淀没有影响。在鱼精蛋白存在的情况下,不仅纤维蛋白原有沉淀,纤维蛋白单体也有沉淀。这些结果表明鱼精蛋白直接与纤维蛋白原(纤维蛋白单体)的d结构域结合导致沉淀。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Protamine interacts with the D-domains of fibrinogen

The mechanism of precipitation of fibrinogen in the presence of a basic protein, protamine, has been investigated. The precipitation was clearly inhibited by the addition of Fragment D. Photooxidation of fibrinogen abolished the association caused by thrombin, but it did not affect the precipitation brought about by protamine. Not only fibrinogen but also fibrin monomer precipitated in the presence of protamine. These results led to the conclusion that protamine bound directly with D-domains of fibrinogen (of fibrin monomer) to cause the precipitation.

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