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本文引用的文献

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Some properties of the protein forming the outer fibers of cilia.构成纤毛外部纤维的蛋白质的一些特性。
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ULTRASTRUCTURE OF DEVELOPING MUSCLE CELLS IN THE CHICK EMBRYO.鸡胚中发育肌肉细胞的超微结构
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ELECTRON MICROSCOPE STUDIES ON THE STRUCTURE OF NATURAL AND SYNTHETIC PROTEIN FILAMENTS FROM STRIATED MUSCLE.横纹肌天然及合成蛋白细丝结构的电子显微镜研究
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The binding of H-meromyosin on crossstriated myofibrils.重酶解肌球蛋白与横纹肌肌原纤维的结合。
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Cell motility by labile association of molecules. The nature of mitotic spindle fibers and their role in chromosome movement.通过分子的不稳定结合实现细胞运动。有丝分裂纺锤体纤维的性质及其在染色体移动中的作用。
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在多种细胞类型中与重酶解肌球蛋白形成箭头状复合物。

Formation of arrowhead complexes with heavy meromyosin in a variety of cell types.

作者信息

Ishikawa H, Bischoff R, Holtzer H

出版信息

J Cell Biol. 1969 Nov;43(2):312-28.

PMID:5344150
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2107852/
Abstract

Heavy meromyosin (HMM) forms characteristic arrowhead complexes with actin filaments in situ. These complexes are readily visualized in sectioned muscle. Following HMM treatment similar complexes appear in sectioned fibroblasts, chondrogenic cells, nerve cells, and several types of epithelial cells. Thin filaments freshly isolated from chondrogenic cells also bind HMM and form arrowhead structures in negatively stained preparations. HMM-filament complexes are prominent in the cortex of a variety of normal metaphase and Colcemid-arrested metaphase cells. There is no detectable binding of HMM with other cellular components such as microtubules, 100-A filaments, tonofilaments, membranes, nuclei, or collagen fibrils. The significance of HMM-filament binding is discussed in view of the finding that arrowhead complexes form in types of cells not usually thought to contain actin filaments.

摘要

重酶解肌球蛋白(HMM)在原位与肌动蛋白丝形成特征性的箭头状复合物。这些复合物在切片肌肉中很容易观察到。用HMM处理后,类似的复合物出现在切片的成纤维细胞、软骨生成细胞、神经细胞和几种类型的上皮细胞中。从软骨生成细胞中新鲜分离出的细肌丝也能结合HMM,并在负染标本中形成箭头状结构。HMM-丝复合物在各种正常中期和秋水仙酰胺阻滞的中期细胞的皮质中很突出。未检测到HMM与其他细胞成分如微管、100 Å丝、张力丝、膜、细胞核或胶原纤维有结合。鉴于在通常不被认为含有肌动蛋白丝的细胞类型中形成了箭头状复合物这一发现,讨论了HMM-丝结合的意义。