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首页> 外文期刊>Journal of Structural Biology >THE STRUCTURE OF THE CONTRACTILE APPARATUS IN ULTRARAPIDLY FROZEN SMOOTH MUSCLE - FREEZE-FRACTURE, DEEP-ETCH, AND FREEZE-SUBSTITUTION STUDIES
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THE STRUCTURE OF THE CONTRACTILE APPARATUS IN ULTRARAPIDLY FROZEN SMOOTH MUSCLE - FREEZE-FRACTURE, DEEP-ETCH, AND FREEZE-SUBSTITUTION STUDIES

机译：超快速冷冻的平滑肌中收缩装置的结构-冷冻断裂，深度腐蚀和冷冻替代研究

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The structure of the smooth muscle contractile apparatus was studied using ultrarapid freezing followed by freeze substitution or by longitudinal freeze-fracture, deep-etch, and platinum-carbon replication. Freeze substitution minimises the detrimental effects of chemical fixation and freeze fracture eliminates them entirely whilst revealing the ultrastructure in three dimensions. Unidirectionally shadowed freeze-fracture replicas of ultrarapidly frozen, relaxed, intact smooth muscle showed a well-preserved actin filament structure; the 5.5-nm repeat of the actin subunits was clearly observed. In transversely fractured tissue the thick filaments were revealed, with a distribution comparable to that seen in transverse sections of freeze-substituted muscle. Relaxed muscle permeabilised using Triton X-100 showed a similar structure to that of intact tissue after ultrarapid freezing and examination both by freeze fracture and by freeze substitution; the ratios of actin to myosin were also comparable. In permeabilised, rigorised tissue the structure of the actomyosin complex was revealed in detail; this was especially clear in freeze-substituted muscle. A cross-bridge spacing of 38 nm was measured in freeze-fractured, deep-etched tissue. The structural detail revealed is compatible with a side polar model of the actomyosin interaction and with the sliding filament mechanism of muscle contraction. (C) 1995 Academic Press, Inc. [References: 40]
机译：使用超快速冷冻，冷冻替代或纵向冷冻断裂，深蚀刻和铂碳复制研究了平滑肌收缩装置的结构。冷冻替代最大程度地减少了化学固定的不利影响，冷冻断裂完全消除了它们，同时在三个维度上揭示了超微结构。超速冷冻，松弛，完整的平滑肌的单向阴影冷冻断裂复制品显示出保存完好的肌动蛋白丝结构。清晰观察到肌动蛋白亚基的5.5 nm重复序列。在横向骨折的组织中，露出了粗丝，其分布与冷冻替代肌肉的横截面中的分布相当。用Triton X-100透化的松弛肌肉在超快速冷冻和通过冷冻断裂和冷冻替代检查后表现出与完整组织相似的结构。肌动蛋白与肌球蛋白的比例也相当。在透化，严格的组织中，放线菌素复合物的结构被详细揭示。在冷冻替代的肌肉中尤其明显。在冷冻断裂的深蚀刻组织中测得的跨桥间距为38 nm。揭示的结构细节与肌动球蛋白相互作用的侧面极性模型以及肌肉收缩的滑动丝机制兼容。 （C）1995 Academic Press，Inc. [参考：40]

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