Roveri N, Ripamonti A, Bigi A, Volpin D, Giro M G
Biochim Biophys Acta. 1979 Feb 26;576(2):404-8. doi: 10.1016/0005-2795(79)90415-x.
The wide angle X-ray diffraction pattern of air-dried lens capsule collagen under tension is the same as the tendon collagen diffraction pattern with regard to the main reflections, and indicates that lens capsule collagen has the characteristic three-stranded helical structure with an axial repeat of 0.29 nm as tendon collagen. The low angle X-ray diffraction pattern shows several weak diffraction maxima corresponding to the meridional reflections of capsule collagen which show orders of 63.0 nm periodicity. This is an evidence of quarter staggered molecular assembly typical of tendon collagen even if less ordered. The results are consistent with the existence in lens capsule collagen of clearly defined molecular units, which can be oriented by stress and are packed in a poor-ordered fibrillar assembly.
拉伸状态下空气干燥的晶状体囊膜胶原蛋白的广角X射线衍射图谱，就主要反射而言，与肌腱胶原蛋白的衍射图谱相同，这表明晶状体囊膜胶原蛋白具有与肌腱胶原蛋白相同的特征性三股螺旋结构，轴向重复距离为0.29纳米。低角度X射线衍射图谱显示出几个与囊膜胶原蛋白的子午线反射相对应的弱衍射极大值，这些反射呈现出63.0纳米周期性的级数。这证明了即使晶状体囊膜胶原蛋白的有序程度较低，但仍具有肌腱胶原蛋白典型的四分之一交错分子组装结构。结果与晶状体囊膜胶原蛋白中存在明确定义的分子单元相一致，这些分子单元可通过应力定向，并以排列不佳的纤维状组装形式堆积。
