Fornieri C, Ronchetti I P, Edman A C, Sjöström M
J Microsc. 1982 Apr;126(Pt 1):87-93. doi: 10.1111/j.1365-2818.1982.tb00359.x.
Cryomethods were used in order to investigate the ultrastructure of native elastin fibres from beef ligamentum nuchae. Filaments of diameter 5 nm, running almost in parallel in purified, negatively-stained elastin preparations, were also seen running along the elastin fibre both in freeze-fractured and etched elastin, that had been stretched up to 200%, and in cryo-sectioned elastin that had been stretched and chemically fixed before freezing. Interconnections between elastin filaments were revealed by the freeze-etching technique. Glycerol treatment, which probably leads to hydration of specimens, resulted, however, in disorganization of filaments and swelling of the elastin fibre. In conclusion, by the use of cryotechniques, it was convincingly demonstrated that elastin molecules are arranged in long interconnecting filaments of about 4-5 nm width.
采用冷冻方法研究牛项韧带中天然弹性蛋白纤维的超微结构。在纯化的、经负染色的弹性蛋白制剂中,直径为5纳米的细丝几乎平行排列,在拉伸至200%的冷冻断裂和蚀刻弹性蛋白中,以及在冷冻前已拉伸并化学固定的冷冻切片弹性蛋白中,也可见这些细丝沿弹性蛋白纤维排列。通过冷冻蚀刻技术揭示了弹性蛋白细丝之间的相互连接。然而,甘油处理可能导致标本水化,结果导致细丝无序排列和弹性蛋白纤维肿胀。总之,通过使用冷冻技术,令人信服地证明弹性蛋白分子排列成宽度约为4-5纳米的长互连细丝。