Matsushima A, Takiuchi H, Saito Y, Inada Y
Biochim Biophys Acta. 1980 Oct 21;625(2):230-6. doi: 10.1016/0005-2795(80)90286-x.
The modification of fibrin monomer with H2O2 caused reduction of the association activity of fibrin monomer. The association activity was not reduced even by modification of approx. 16 out of the total 64 tryptophan residues in the fibrin molecule; it was then abolished by further modification of the following several residues. Fragment D obtained by proteolysis of fibrinogen with plasmin, inhibited the association activity of fibrin monomer and the modification of approx. six out of the total 21 tryptophan residues in the fragment led to the complete loss of the inhibitory effect. It was concluded from these studies that about six tryptophan residues in the D-domain of fibrin are important for the association of fibrin monomer.
用过氧化氢对纤维蛋白单体进行修饰，会导致纤维蛋白单体的聚合活性降低。即使对纤维蛋白分子中总共64个色氨酸残基中的约16个进行修饰，聚合活性也不会降低；但对接下来的几个残基进一步修饰后，聚合活性就会被消除。用纤溶酶对纤维蛋白原进行蛋白水解得到的D片段，抑制了纤维蛋白单体的聚合活性，并且对该片段中总共21个色氨酸残基中的约6个进行修饰会导致抑制作用完全丧失。从这些研究得出的结论是，纤维蛋白D结构域中的约6个色氨酸残基对纤维蛋白单体的聚合很重要。
