Timme A H
J Anat. 1978 Oct;127(Pt 2):415-24.
Erythroycte ghosts fixed in glutaraldehyde were dehydrated in (a) alcohol or acetone, (b) propylene glycol followed by Epon and embedded in an epoxy resin. A water-soluble urea/glutaraldehyde mixture was also used. The aim was to study the structure of the peripheral protein layer, which contains spectrin and actin, in the absence of OsO4 induced denaturation changes. Ghost membranes prepared in this way had an asymmetrical quadrilaminar structure. A layer of amorphous peripheral protein +/- 18 nm in width covered the entire inner face of the membrane in the form of a coarse meshwork in both Wash I (haemoglobin-containing) and haemoglobin-free ghosts. Cations (Mg2+ or Ca2+, or Mg2+ plus ATP) had no apparent effect on its fine structure. In contrast, the corresponding layer in OsO4-fixed membranes was represented by scanty, fuzzy material attached to the unit membrane only at irregular intervals. The results demonstrate the superior ability of glutaraldehyde to preserve the peripheral protein layer in thin sections, and afford further support for the view that much of this protein normally exists in an unpolymerized state.
用戊二醛固定的红细胞血影在（a）酒精或丙酮中脱水，（b）先在丙二醇中脱水，然后用环氧树脂包埋。也使用了一种水溶性尿素/戊二醛混合物。目的是在不存在四氧化锇诱导的变性变化的情况下，研究包含血影蛋白和肌动蛋白的外周蛋白层的结构。以这种方式制备的血影膜具有不对称的四边形结构。在洗涤I（含血红蛋白）和不含血红蛋白的血影中，一层宽度约为18纳米的无定形外周蛋白以粗糙网络的形式覆盖在膜的整个内表面。阳离子（镁离子或钙离子，或镁离子加三磷酸腺苷）对其精细结构没有明显影响。相比之下，在四氧化锇固定的膜中，相应的层仅以不规则间隔附着在单位膜上的少量模糊物质为代表。结果表明，戊二醛在保存薄片中外周蛋白层方面具有卓越能力，并进一步支持了这样一种观点，即这种蛋白的大部分通常以未聚合状态存在。
