Trachtenberg S
Biochim Biophys Acta. 1987 Mar 19;923(3):327-32. doi: 10.1016/0304-4165(87)90039-0.
Protein extracts from normal human epidermis reassemble in vitro into 8-10 nm diameter filaments characteristic of intermediate filaments, whereas extracts from psoriatic epidermal scales reassemble, under identical conditions, into a variety of paracrystalline bundles. Optical diffraction and image analysis of these paracrystalline bundles reveal an axial repeat of 16.5 nm, which subdivides into three bands of 5.5 nm, and a lateral spacing of 5.1 nm. This information, together with available sequence studies of intermediate filaments and biochemical data, suggests that the subunit of psoriatic keratin is made up essentially from the coiled-coil alpha-helical rod domain of the normal keratin subunits, whereas the random coil domains are missing or greatly reduced in size.
正常人表皮的蛋白质提取物在体外重新组装成直径为8 - 10纳米的中间丝特征性细丝，而在相同条件下，银屑病表皮鳞屑提取物则重新组装成各种准晶体束。对这些准晶体束的光学衍射和图像分析显示，轴向重复距离为16.5纳米，可细分为三个5.5纳米的带，横向间距为5.1纳米。这些信息，连同中间丝的现有序列研究和生化数据表明，银屑病角蛋白的亚基基本上由正常角蛋白亚基的卷曲螺旋α-螺旋杆结构域组成，而无规卷曲结构域缺失或尺寸大大减小。
