Medved' L V, Gorkun O V, Manyakov V F, Belitser V A
FEBS Lett. 1985 Feb 11;181(1):109-12. doi: 10.1016/0014-5793(85)81123-6.
Turbidity development registration and electron microscopic observation of the assembly process of the fibrin monomer and its derivative lacking in intact alpha C-domains (monomeric X1 fragment) have shown that these domains participate in fibrin polymerization, not as structural components, but as a factor promoting the ordered process of fibrin assembly.
对纤维蛋白单体及其缺乏完整αC结构域的衍生物(单体X1片段)组装过程的浊度发展记录和电子显微镜观察表明,这些结构域参与纤维蛋白聚合,并非作为结构成分,而是作为促进纤维蛋白组装有序过程的一个因素。