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首页> 外文期刊>Journal of Molecular Biology >Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy.
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Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy.

机译：通过冷冻电子显微镜研究离体淀粉样蛋白原纤维的结构多样性。

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摘要

Cryo-electron microscopy studies are presented on amyloid fibrils isolated from amyloidotic organs of two patients with different forms of hereditary non-neuropathic systemic amyloidosis, caused, respectively, by Leu60Arg apolipoprotein AI and Asp67His lysozyme. Although ex vivo amyloid fibrils were thought to be more uniform in structure than those assembled in vitro, our findings show that these fibrils are also quite variable in structure. Structural disorder and variability of the fibrils have precluded three-dimensional reconstruction, but averaged cryo-electron microscopy images suggest models for protofilament packing in the lysozyme fibrils. We conclude that ex vivo amyloid fibrils, although variable, assemble as characteristic structures according to the identity of the precursor protein. Copyright 2001 Academic Press.
机译：低温电子显微镜研究显示了从两名分别由Leu60Arg载脂蛋白AI和Asp67His溶菌酶引起的具有不同形式的遗传性非神经性系统性淀粉样变性的两名患者的淀粉样变性器官分离的淀粉样蛋白原纤维。尽管人们认为离体淀粉样蛋白原纤维的结构比体外组装的更为均匀，但我们的发现表明，这些原纤维的结构也存在很大差异。原纤维的结构紊乱和变异性阻止了三维重建，但是平均的冷冻电子显微镜图像显示了溶菌酶原纤维中原丝堆积的模型。我们得出结论，离体淀粉样蛋白原纤维尽管可变，但根据前体蛋白的身份组装为特征结构。版权所有2001，学术出版社。

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