Measurement of work done by ATP‐induced sliding between rabbit muscle myosin and algal cell actin cables in vitro.
Measurement of work done by ATP‐induced sliding between rabbit muscle myosin and algal cell actin cables in vitro.
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体外测量 ATP 诱导的兔肌肉肌球蛋白和藻细胞肌动蛋白电缆之间滑动所做的功。
DOI：
10.1113/jphysiol.1991.sp018623
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Haruo Sugi
中科院分区：
文献类型：
--
作者：
Kazuhiro Oiwa;S. Chaen;Haruo Sugi
1.利用体外作用力-运动分析系统，研究了ATP依赖的肌动蛋白-肌球蛋白相互作用引起肌肉收缩的基本性质。2.对三磷酸腺苷电流脉冲(强度5~85 nA，持续时间0.5~10 S)的反应，肌球蛋白包被的针移动了一段距离并最终停止，这表明肌动蛋白-肌球蛋白的僵硬连接重新形成，以防止弯曲的针的弹性反冲。随后的ATP电流脉冲再次产生从前一针运动所获得的基线力开始的针运动。3.ATP加入量不变时，肌动蛋白-肌球蛋白滑动量随基线力从0增加到0.4-0.6P0而先增加，然后随基线力进一步增加而减少，呈现钟形功与基线力的关系。4.随着ATP施用量的增加，当基线力从0增加到0.4-0.6P0时，肌动蛋白-肌球蛋白滑动量的增加幅度更大。5.结合肌动蛋白-肌球蛋白在肌肉收缩中滑动的基本性质讨论了这些结果。
1. The basic properties of the ATP‐dependent actin‐myosin interaction responsible for muscle contraction were studied using an in vitro force‐movement assay system, in which a glass microneedle coated with rabbit skeletal muscle myosin was made to slide on the actin filament arrays (actin cables) in the internodal cell of an alga Nitellopsis obtusa with ionophoretic application of ATP. 2. In response to an ATP current pulse (intensity, 5‐85 nA; duration, 0.5‐10 s), the myosin‐coated needle moved for a distance and eventually stopped, indicating reformation of rigor actin‐myosin linkages to prevent elastic recoil of the bent needle. A subsequent ATP current pulse again produced the needle movement starting from the baseline force attained by the preceding needle movement. 3. With a constant amount of ATP application, the amount of work done by the ATP‐induced actin‐myosin sliding first increased with increasing baseline force from zero to 0.4‐0.6P0, and then decreased with further increasing baseline force, thus giving a bell‐shaped work versus baseline force relation. 4. With increasing amount of ATP application, the amount of work done by the actin‐myosin sliding increased more steeply as the baseline force was increased from zero to 0.4‐0.6P0. 5. These results are discussed in connection with the basic properties of the actin‐myosin sliding in muscle contraction.
DOI：
10.1073/pnas.83.17.6272
发表时间：
1986-09-01
影响因子：
11.1
作者：
KRON, SJ;SPUDICH, JA
通讯作者：
SPUDICH, JA