The relation of muscle biochemistry to muscle physiology.
The relation of muscle biochemistry to muscle physiology.
复制标题
肌肉生物化学与肌肉生理学的关系。
DOI：
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发表时间：
1980
影响因子：
18.2
通讯作者：
L. Greene
中科院分区：
文献类型：
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作者：
E. Eisenberg;L. Greene
在过去的几年里，肌肉收缩领域的主要挑战是发展一个详细的理论来解释肌肉如何产生力量和做功。现在人们普遍认为，肌肉收缩的整体机制涉及粗肌球蛋白细丝滑过细肌动蛋白细丝，这是由ATP水解驱动的过程（29，31）。大多数研究者也同意，这种滑动过程是由肌动蛋白丝与肌球蛋白丝延伸的横桥的循环相互作用引起的（28，29，31）。然而，这种循环相互作用的细节仍然难以捉摸。从结构、生理和生化的角度研究了肌球蛋白跨桥与肌动蛋白丝的循环相互作用。这篇评论讨论了如何这三种观点可能是统一在一个跨桥行动的单一观点。而不是试图详尽的文献综述，我们专注于各种生化模型提出的肌动球蛋白ATP酶，以及它们如何与肌肉收缩的机制。此外，提出了一种新的模型，在体内的跨桥行动，基于一个生化模型，似乎最适合目前的生化数据。
During the last several years, the major challenge in the field of muscle contraction has been to develop a detailed theory explaining how muscle develops force and produces work. There is now general agreement that the overall mechanism of muscle contraction involves the sliding of the thick myosin filaments past the thin actin filaments, a process driven by the hydrolysis of ATP (29, 31). Most workers also agree that this sliding process is caused by a cyclic interaction of the actin filaments with cross-bridges extending from the myosin filament (28, 29, 31). However, the details of this cyclic interaction remain elusive. The cyclic interaction of the myosin cross-bridges with the actin filaments has been investigated from structural, physiological, and biochemical view points. This review discusses how these three viewpoints might be united in a single view of cross-bridge action . Rather than attempt an exhaustive review of the literature, we focus on various biochemical models proposed for the actomyosin ATPase and how they relate to the mechanism of muscle contraction. In addition, a new model of cross-bridge action in vivo is presented, based on a biochemical model that appears to fit best the current biochemical data.