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人类胰岛淀粉样变。II. 分离淀粉样物质的电子显微镜分析。

Amyloid of human islets of Langerhans. II. Electron microscopic analysis of isolated amyloid.

作者信息

Westermark P

出版信息

Virchows Arch A Pathol Anat Histol. 1977 Mar 11;373(2):161-6. doi: 10.1007/BF00432160.

Abstract

Isolated amyloid from the islets of Langerhans of patients with maturity onset diabetes mellitus was compared with amyloid fibrils from patients with different types of systemic amyloidosis. It was found that systemic amyloids had in common rigid and non-branching filaments with a width of about 75 A and that these filaments sometimes were attached laterally, forming thicker fibrils. Similar filaments could also be extracted from islet amyloid but the main part of this amyloid was built up by large aggregates of very thin and often very wavy units. This structure, which has not been previously described in human amyloid, probably explains some properties of isolated islet amyloid.

摘要

将成年型糖尿病患者胰岛中分离出的淀粉样蛋白与不同类型系统性淀粉样变性患者的淀粉样纤维进行了比较。结果发现,系统性淀粉样蛋白具有共同特征,即由宽度约为75埃的刚性且无分支的细丝组成,这些细丝有时会侧向附着,形成更粗的纤维。类似的细丝也可以从胰岛淀粉样蛋白中提取出来,但这种淀粉样蛋白的主要部分是由非常细且通常非常弯曲的单元大量聚集而成。这种结构在人类淀粉样蛋白中此前未曾描述过,可能解释了分离出的胰岛淀粉样蛋白的一些特性。

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