ON STRUCTURE OF RESILIN
ON STRUCTURE OF RESILIN
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DOI：
10.1016/s0022-2836(65)80144-9
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发表时间：
1965-01-01
影响因子：
5.6
通讯作者：
WEISFOGH, T
中科院分区：
文献类型：
--
作者：
ELLIOTT, GF;HUXLEY, AF;WEISFOGH, T
由橡胶样蛋白质节枝弹性蛋白组成的昆虫结构已经通过高角和低角X射线衍射和电子显微镜中的薄片进行了检查。通过X-射线衍射，纯节枝弹性蛋白的腱，在没有张力的情况下风干，在约4 A下得到弥散的未取向环。在张力下干燥的肌腱，在2[middot]6到3[middot]3倍的无应变长度下，产生相同的环，此外，在4-5 [±] 005 A处产生单一的赤道反射。当肌腱恢复到未拉紧长度时，反射消失。在任何时候都没有观察到低角度反射。由节枝弹性蛋白组成的结构不被甲基丙烯酸酯穿透，但获得的切片含有被甲基丙烯酸酯包围的纯节枝弹性蛋白的斑块。在电子显微镜下，这些切片显示用四氧化锇处理的节枝弹性蛋白具有低的电子散射能力，并且没有可检测到的精细结构。因此，由节枝弹性蛋白形成的小结构极难检测。这两种方法都表明节枝弹性蛋白是高度无定形的，正如从其物理性质所预期的那样。
Structures from insects composed of the rubber-like protein resilin have been examined by high- and low-angle X-ray diffraction and in thin sections in the electron microscope. By X-ray diffraction, tendons of pure resilin, air-dried without tension, gave a diffuse unoriented ring at about 4 A. Tendons dried under tension, at 2[middot]6 to 3[middot]3 times unstrained length, gave the same ring and in addition a single equatorial reflection at 4-5 [plus or minus] 005 A. This reflection disappeared when the tendon was returned to its unstrained length. No low-angle reflections were observed at any time. Structures composed of resilin were not penetrated by methacrylate, but sections were obtained containing patches of pure resilin surrounded by methacrylate. In the electron microscope, these sections showed that resilin treated with osmium tetroxide has a low electron-scattering power and no detectable fine structure. Small structures formed of resilin would therefore be extremely difficult to detect. Both methods show resilin to be highly amorphous, as was to be expected from its physical properties.