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本文引用的文献

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Theoretical model for the cooperative equilibrium binding of myosin subfragment 1 to the actin-troponin-tropomyosin complex.肌球蛋白亚片段1与肌动蛋白-肌钙蛋白-原肌球蛋白复合物协同平衡结合的理论模型。
Proc Natl Acad Sci U S A. 1980 Jun;77(6):3186-90. doi: 10.1073/pnas.77.6.3186.
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Cooperative binding of myosin subfragment-1 to the actin-troponin-tropomyosin complex.肌球蛋白亚片段-1与肌动蛋白-肌钙蛋白-原肌球蛋白复合物的协同结合。
Proc Natl Acad Sci U S A. 1980 May;77(5):2616-20. doi: 10.1073/pnas.77.5.2616.
3
Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.肌钙蛋白-原肌球蛋白对肌动球蛋白ATP酶活性的抑制作用,而不阻断肌球蛋白与肌动蛋白的结合。
J Biol Chem. 1982 Mar 10;257(5):2432-7.
4
Pressure-relaxation studies of pyrene-labelled actin and myosin subfragment 1 from rabbit skeletal muscle. Evidence for two states of acto-subfragment 1.兔骨骼肌中芘标记的肌动蛋白和肌球蛋白亚片段1的压力松弛研究。肌动蛋白-亚片段1两种状态的证据。
Biochem J. 1985 Dec 1;232(2):351-6. doi: 10.1042/bj2320351.
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Two-step ligand binding and cooperativity. A model to describe the cooperative binding of myosin subfragment 1 to regulated actin.两步配体结合与协同性。一种描述肌球蛋白亚片段1与调节型肌动蛋白协同结合的模型。
Biophys J. 1987 Aug;52(2):215-20. doi: 10.1016/S0006-3495(87)83208-3.
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Transient tension changes initiated by laser temperature jumps in rabbit psoas muscle fibres.激光温度跃升引发的兔腰大肌纤维中的瞬态张力变化。
J Physiol. 1987 Nov;392:71-95. doi: 10.1113/jphysiol.1987.sp016770.
7
Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction.钙离子对去皮肤的单根兔腰大肌纤维横桥转换动力学的影响:对肌肉收缩调节的意义。
Proc Natl Acad Sci U S A. 1988 May;85(9):3265-9. doi: 10.1073/pnas.85.9.3265.
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Tension responses to increased hydrostatic pressure in glycerinated rabbit psoas muscle fibres.
Proc R Soc Lond B Biol Sci. 1987 Nov 23;232(1267):217-26. doi: 10.1098/rspb.1987.0070.
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Pressure sensitivity of active tension in glycerinated rabbit psoas muscle fibres: effects of ADP and phosphate.
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10
Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle.哺乳动物去表皮骨骼肌纤维中肌球蛋白磷酸化与横桥附着速率及张力的变化。对完整肌肉中强直收缩增强的影响。
J Gen Physiol. 1989 May;93(5):855-83. doi: 10.1085/jgp.93.5.855.

去皮肤兔肌纤维的收缩激活与力产生:流体静压力的影响

Contractile activation and force generation in skinned rabbit muscle fibres: effects of hydrostatic pressure.

作者信息

Fortune N S, Geeves M A, Ranatunga K W

机构信息

Department of Physiology, School of Medicine, University of Bristol.

出版信息

J Physiol. 1994 Jan 15;474(2):283-90. doi: 10.1113/jphysiol.1994.sp020021.

DOI:10.1113/jphysiol.1994.sp020021
PMID:8006815
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1160317/
Abstract
  1. Effects of hydrostatic pressure (range 0.1-10 MPa) on the isometric tension of skinned (rabbit psoas) muscle fibres were examined at 12 degrees C and at different levels of Ca2+ activation (pCa range 4-7); the effects on both the steady tension and the tension transients induced by rapid pressure release (< 1 ms) are described. 2. The steady tension was depressed by increased pressure (approximately 1% MPa-1) at a high level of Ca2+ activation (pCa approximately 4) whereas it was potentiated at lower Ca2+ levels (pCa > 6); the effects were reversible. 3. At maximal Ca2+ activation, the tension recovery following pressure release (10 MPa to atmospheric) consisted of a fast (approximately 30 s-1) and a slow (2-3 s-1) phase; the rate and the normalized amplitude (normalized to the steady tension at atmospheric pressure for a particular pCa) of the fast phase were invariant with changes in Ca2+ level. 4. The effects of changing Ca2+ level on the slow phase were complex; its positive amplitude at high Ca2+ levels changed to negative and the rate decreased to approximately 1 s-1 at low Ca2+ levels (pCa > 6.0). 5. Results are discussed in relation to previous studies on the effect of pressure on intact muscle fibres and the actin-myosin interaction. This work supports calcium regulation of cross-bridge recruitment rather than calcium regulation of the rate of a specific step in the cross-bridge cycle.
摘要
  1. 在12摄氏度以及不同的Ca2+激活水平(pCa范围为4 - 7)下,研究了静水压力(范围为0.1 - 10兆帕)对去膜(兔腰大肌)肌纤维等长张力的影响;描述了对稳定张力以及快速压力释放(<1毫秒)引起的张力瞬变的影响。2. 在高Ca2+激活水平(pCa约为4)时,稳定张力随压力增加而降低(约1%兆帕-1),而在较低Ca2+水平(pCa > 6)时则增强;这些影响是可逆的。3. 在最大Ca2+激活时,压力释放(从10兆帕降至大气压)后的张力恢复包括一个快速(约30秒-1)和一个缓慢(2 - 3秒-1)阶段;快速阶段的速率和归一化幅度(相对于特定pCa下大气压时的稳定张力进行归一化)不随Ca2+水平变化而改变。4. Ca2+水平变化对缓慢阶段的影响较为复杂;在高Ca2+水平时其正向幅度变为负向,且在低Ca2+水平(pCa > 6.0)时速率降至约1秒-1。5. 结合先前关于压力对完整肌纤维和肌动蛋白-肌球蛋白相互作用影响的研究对结果进行了讨论。这项工作支持了钙离子对横桥募集的调节,而非对横桥循环中特定步骤速率的钙离子调节。