ULTRASTRUCTURE OF HUMAN AMYLOID AS REVEALED BY NEGATIVE STAINING TECHNIQUE
ULTRASTRUCTURE OF HUMAN AMYLOID AS REVEALED BY NEGATIVE STAINING TECHNIQUE
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DOI：
10.1016/s0022-5320(66)80075-8
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发表时间：
1966-01-01
期刊：
影响因子：
--
通讯作者：
GLENNER, GG
中科院分区：
文献类型：
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作者：
BLADEN, HA;NYLEN, MU;GLENNER, GG
富含淀粉样蛋白的组织取自五名原发性或继发性淀粉样变性患者。通过差速离心过程分离淀粉样蛋白，并使用负染色技术在电子显微镜中进行检查。所有制剂中都存在两种类型的颗粒，一种是 100 A 宽的棒状颗粒，另一种是直径 90 A 的小五边形结构（单元结构）。窄的电子致密带将杆以规则的间隔分成较小的片段，使得它们呈现出具有大约40A的周期性的交叉条纹。然而，致密带的宽度经常变化，这表明这些片段很容易分裂。单元结构似乎是平躺的单个片段，因此提供了淀粉样蛋白棒的端视图。它们似乎由围绕致密核心的 5 个球状部分组成，表明淀粉样蛋白棒是中空结构，可能由一系列球状单元组成。
Amyloid-laden tissue was obtained from five patients with either primary or secondary amyloidosis. The amyloid was isolated through a process of differential centrifugation and was examined inthe electronmicrosqppeusingnegative-stainingtechniques. Two types of particles, one a 100 A wide rod, the other a small pentagonal structure (unit structure) 90 A in diameter, present in all preparations. Narrow electron dense bands divided the rods at regular intervals into smaller segments so that they appeared cross- striated with a periodicity of approximately 40 A. Frequently, however, the dense bands varied in width, suggesting that the segments were easily disunited. The unit structures seemed to be single segments lying on their flat side, thus affording an end view of the amyloid rod. They appeared to be composed of 5 globular sections surrounding a dense core, indicating that the amyloid rods were hollow structures possibly consisting of an array of globular units.