HODGE A J
J Biophys Biochem Cytol. 1956 Jul 25;2(4 Suppl):131-42. doi: 10.1083/jcb.2.4.131.
The available evidence from phase contrast, polarization optical, and electron microscopic studies on vertebrate skeletal muscle, insect skeletal muscle, and dipteran flight muscle is interpreted as favoring the following general structure of striated muscle. A continuous array of filaments (actin) runs through all bands of the sarcomere. These are linked by an axially periodic system of transverse filamentous bridges. Myosin (and probably other substances) are localized in the A bands. The system of transverse bridges compensates the birefringence of actin and is thus responsible for the isotropy of the I band. Myosin is responsible for the birefringence of the A bands. On strong contraction, A band material migrates to the Z bands to form contraction bands. It is not yet certain whether this migration involves myosin or another A band component.
来自对脊椎动物骨骼肌、昆虫骨骼肌和双翅目飞行肌的相衬显微镜、偏振光学显微镜和电子显微镜研究的现有证据表明，横纹肌的一般结构如下。一系列连续的细丝（肌动蛋白）贯穿肌节的所有带。这些细丝通过横向丝状桥的轴向周期性系统相连。肌球蛋白（可能还有其他物质）定位于A带。横向桥系统补偿了肌动蛋白的双折射，因此导致I带的各向同性。肌球蛋白导致A带的双折射。在强烈收缩时，A带物质迁移到Z带形成收缩带。目前尚不确定这种迁移涉及的是肌球蛋白还是A带的其他成分。
