Dahlbäck B
J Biol Chem. 1985 Feb 10;260(3):1347-9.
Purified single-chain human coagulation factor V (Mr approximately 330,000) was visualized by high-resolution transmission electron microscopy. The molecule was found to be composed of four major domains. Three similar sized (approximately 90 X 70 A) globular domains were linked via thin (approximately 30 A) spacers to a somewhat larger (approximately 165 X 138 A) central domain. The center-to-center distances between the larger central domain and each of the peripheral domains were found to be approximately 120 A. Incubation of factor V with thrombin resulted in a separation of the peripheral domains from the central domain. This indicates that the factor V domains now observed correspond to the previously characterized factor V fragments formed by limited proteolysis using thrombin. From these results, a model of the three-dimensional factor V structure, distinct from previous models, is proposed.
通过高分辨率透射电子显微镜观察纯化的单链人凝血因子V（分子量约330,000）。发现该分子由四个主要结构域组成。三个大小相似（约90×70埃）的球形结构域通过细（约30埃）的间隔区与一个稍大（约165×138埃）的中央结构域相连。发现较大的中央结构域与每个外周结构域之间的中心距约为120埃。凝血酶与因子V孵育导致外周结构域与中央结构域分离。这表明现在观察到的因子V结构域对应于先前使用凝血酶通过有限蛋白水解形成的因子V片段。基于这些结果，提出了一种与先前模型不同的三维因子V结构模型。
