脊椎动物平滑肌组织切片中肌球蛋白的定位与聚集状态。
Locus and state of aggregation of myosin in tissue sections of vertebrate smooth muscle.
作者信息
Panner B J, Honig C R
出版信息
J Cell Biol. 1970 Jan;44(1):52-61. doi: 10.1083/jcb.44.1.52.
Abstract
Structures with the characteristics of molecular myosin were identified by electron microscopy in tissue sections of vertebrate smooth muscle. No thick filaments of myosin were found regardless of preparative procedures, which included fixation at rest and in contraction, glycerine extraction, and storage at low pH prior to fixation. Absence of thick myosin filaments and presence of what appear to be myosin molecules is in accord with conclusions based on X-ray diffraction (3, 12) and birefringence data (4) from living smooth muscles at rest and in contraction. Explanations are provided for appearances thought by others (6, 20, 21) to represent thick myosin filaments. Our present observations are in accord with the model for smooth muscle contraction which we have previously proposed (1).
摘要
通过电子显微镜在脊椎动物平滑肌组织切片中鉴定出具有分子肌球蛋白特征的结构。无论采用何种制备程序，均未发现肌球蛋白粗丝，这些程序包括在静止和收缩状态下固定、甘油提取以及在固定前在低pH值下储存。肌球蛋白粗丝的缺失以及看似肌球蛋白分子的存在与基于对静止和收缩状态下的活平滑肌进行X射线衍射（3,12）和双折射数据（4）得出的结论一致。对其他人（6,20,21）认为代表肌球蛋白粗丝的外观给出了解释。我们目前的观察结果与我们之前提出的平滑肌收缩模型（1）一致。
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