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Formation of a ternary complex: actin, 5'-adenylyl imidodiphosphate, and the subfragments of myosin.三元复合物的形成：肌动蛋白、5'-腺苷酰亚胺二磷酸和肌球蛋白亚片段。
Proc Natl Acad Sci U S A. 1978 Jan;75(1):54-8. doi: 10.1073/pnas.75.1.54.
2
Kinetic and thermodynamic properties of the ternary complex between F-actin, myosin subfragment 1 and adenosine 5'-[beta, gamma-imido]triphosphate.肌动蛋白丝（F-肌动蛋白）、肌球蛋白亚片段1与腺苷5'-[β,γ-亚氨基]三磷酸之间三元复合物的动力学和热力学性质
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3
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4
Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi.肌动蛋白亚片段1复合物被腺苷-5'-亚氨二磷酸、ADP和焦磷酸解离。
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Fluorescence energy transfer between the myosin subfragment-1 isoenzymes and F-actin in the absence and presence of nucleotides.在有无核苷酸存在的情况下，肌球蛋白亚片段-1同工酶与F-肌动蛋白之间的荧光能量转移
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6
The function of two heads of myosin in muscle contraction.肌球蛋白双头在肌肉收缩中的作用。
Adv Exp Med Biol. 1988;226:227-35.
7
The covalent modification of myosin's proteolytic fragments by a purine disulfide analog of adenosine triphosphate. Reaction at a binding site other than the active site.三磷酸腺苷的嘌呤二硫化物类似物对肌球蛋白蛋白水解片段的共价修饰。在活性位点以外的结合位点发生的反应。
Biochemistry. 1975 Nov 18;14(23):5156-62. doi: 10.1021/bi00694a021.
8
Comparison of the binding of heavy meromyosin and myosin subfragment 1 in F-actin.F-肌动蛋白中重酶解肌球蛋白与肌球蛋白亚片段1结合的比较。
Biochemistry. 1981 Apr 14;20(8):2120-6. doi: 10.1021/bi00511a008.
9
Cryoenzymic studies on actomyosin ATPase. Evidence that the degree of saturation of actin with myosin subfragment 1 affects the kinetics of the binding of ATP.肌动球蛋白ATP酶的低温酶学研究。肌动蛋白与肌球蛋白亚片段1的饱和程度影响ATP结合动力学的证据。
Biochemistry. 1990 Feb 20;29(7):1846-52. doi: 10.1021/bi00459a026.
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Effect of ethylene glycol on the interaction of different myosin subfragment 1.nucleotide complexes with actin.乙二醇对不同肌球蛋白亚片段1-核苷酸复合物与肌动蛋白相互作用的影响。
Biochemistry. 1989 Jul 25;28(15):6478-82. doi: 10.1021/bi00441a048.

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1
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Stereochemical aspects of the interaction of myosin and actomyosin with nucleotides.肌球蛋白和肌动球蛋白与核苷酸相互作用的立体化学方面
J Muscle Res Cell Motil. 1980 Mar;1(1):101-15. doi: 10.1007/BF00711928.
6
Evidence for an altered structure of actin-S1 complexes when Mg-adenylylimidodiphosphate binds.当镁-腺苷酰亚胺二磷酸结合时，肌动蛋白-S1复合物结构改变的证据。
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7
Cross-bridge model of muscle contraction. Quantitative analysis.肌肉收缩的横桥模型。定量分析。
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The influence of doubly attached crossbridges on the mechanical behavior of skeletal muscle fibers under equilibrium conditions.在平衡条件下，双附着横桥对骨骼肌纤维力学行为的影响。
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9
Ca2+-sensitive cross-bridge dissociation in the presence of magnesium pyrophosphate in skinned rabbit psoas fibers.在去表皮的兔腰大肌纤维中，焦磷酸镁存在时钙离子敏感的横桥解离
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10
Single-headed binding of a spin-labeled-HMM-ADP complex to F-actin. Saturation transfer electron paramagnetic resonance and sedimentation studies.自旋标记的重链肌球蛋白-ADP复合物与F-肌动蛋白的单头结合。饱和转移电子顺磁共振和沉降研究。
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本文引用的文献

1
Equilibrium binding of adenosine diphosphate to myosin.二磷酸腺苷与肌球蛋白的平衡结合
Biochemistry. 1969 Aug;8(8):3195-9. doi: 10.1021/bi00836a010.
2
Formation of acto-H-meromyosin and acto-subfragment-1 complexes and their dissociation by adenosine triphosphate.肌动蛋白-H-肌球蛋白和肌动蛋白-亚片段1复合物的形成及其被三磷酸腺苷解离。
J Biochem. 1971 Dec;70(6):1011-26. doi: 10.1093/oxfordjournals.jbchem.a129710.
3
Binding of actin to heavy meromyosin in the absence of adenosine triphosphate.在没有三磷酸腺苷的情况下肌动蛋白与重酶解肌球蛋白的结合。
Biochemistry. 1972 Dec 5;11(25):4657-60. doi: 10.1021/bi00775a003.
4
Individual states in the cycle of muscle contraction.肌肉收缩周期中的各个阶段。
Proc Natl Acad Sci U S A. 1972 Sep;69(9):2542-6. doi: 10.1073/pnas.69.9.2542.
5
Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P--N--P linkage.腺苷亚氨基二磷酸，一种含有P-N-P键的三磷酸腺苷类似物。
Biochemistry. 1971 Jun 22;10(13):2484-9. doi: 10.1021/bi00789a009.
6
Binding of adenylyl imidodiphosphate, an analog of adenosine triphosphate, to myosin and heavy meromyosin.腺苷三磷酸类似物腺苷酰亚胺二磷酸与肌球蛋白和重酶解肌球蛋白的结合。
J Biol Chem. 1974 Aug 10;249(15):4985-9.
7
The reversal of the myosin and actomyosin ATPase reactions and the free energy of ATP binding to myosin.肌球蛋白和肌动球蛋白ATP酶反应的逆转以及ATP与肌球蛋白结合的自由能。
Biochem Biophys Res Commun. 1974 Apr 8;57(3):709-16. doi: 10.1016/0006-291x(74)90604-4.
8
Mechanism of adenosine triphosphate hydrolysis by actomyosin.肌动球蛋白水解三磷酸腺苷的机制。
Biochemistry. 1971 Dec 7;10(25):4617-24. doi: 10.1021/bi00801a004.
9
Interaction of P--N--P and P--C--P analogs of adenosine triphosphate with heavy meromyosin, myosin, and actomyosin.三磷酸腺苷的P--N--P和P--C--P类似物与重酶解肌球蛋白、肌球蛋白和肌动球蛋白的相互作用。
Biochemistry. 1971 Jun 22;10(13):2490-6. doi: 10.1021/bi00789a010.
10
Subfragment 1 of myosin: adenosine triphophatase activation by actin.肌球蛋白亚片段1：肌动蛋白对三磷酸腺苷酶的激活作用。
Biochemistry. 1968 Sep;7(9):3186-94. doi: 10.1021/bi00849a022.

三元复合物的形成：肌动蛋白、5'-腺苷酰亚胺二磷酸和肌球蛋白亚片段。

Formation of a ternary complex: actin, 5'-adenylyl imidodiphosphate, and the subfragments of myosin.

作者信息

Greene L E, Eisenberg E

出版信息

Proc Natl Acad Sci U S A. 1978 Jan;75(1):54-8. doi: 10.1073/pnas.75.1.54.

DOI:10.1073/pnas.75.1.54
PMID:343111
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC411182/
Abstract

The formation of the ternary complex composed of actin, 5'-adenylyl imidodiphosphate [AMP-P(NH)P], and myosin subfragment 1 (S-1) was studied using the analytical ultracentrifuge with UV optics, which enabled the direct determination of the extent of dissociation of actin.S-1 (acto.S-1) by AMP-P(NH)P. In contrast to the reaction with ATP, at saturating levels of AMP-P(NH)P (1.5 mM), extensive formation of the ternary acto.S-1.AMP-P(NH)P complex occurs at 22 degrees . With 40 muM actin present, AMP-P(NH)P causes almost no dissociation of the acto.S-1 complex at 0.04 M ionic strength, while even at 0.22 M ionic strength one-third of the S-1 remains associated with actin and AMP-P(NH)P in a ternary complex. A detailed study of the binding of S-1.AMP-P(NH)P to actin using the Scatchard plot analysis shows that, at saturation, 1 mol of S-1.AMP-P(NH)P binds per mol of actin monomer. There appears to be no cooperativity occurring as the S-1.AMP-P(NH)P binds along the actin filament, with the possible exception of a slight positive cooperativity when most of the sites on the actin filament are saturated. The turbidity of the ternary complex is identical to the turbidity of acto.S-1 alone. Preliminary experiments with the two-headed subfragment of myosin, heavy meromyosin (HMM), show that the binding of HMM.AMP-P(NH)P to actin is only about twice as strong as the binding of S-1.AMP-P(NH)P to actin, indicating that the second head contributes very little to the free energy of binding.

摘要

使用配备紫外光学系统的分析超速离心机研究了由肌动蛋白、5'-腺苷酰亚胺二磷酸[AMP-P(NH)P]和肌球蛋白亚片段1（S-1）组成的三元复合物的形成，该系统能够直接测定AMP-P(NH)P引起的肌动蛋白-S-1（肌动蛋白·S-1）解离程度。与ATP反应不同，在AMP-P(NH)P饱和水平（1.5 mM）下，22℃时会大量形成三元肌动蛋白·S-1·AMP-P(NH)P复合物。当存在40 μM肌动蛋白时，在0.04 M离子强度下，AMP-P(NH)P几乎不会导致肌动蛋白·S-1复合物解离，而即使在0.22 M离子强度下，仍有三分之一的S-1与肌动蛋白和AMP-P(NH)P形成三元复合物结合。使用Scatchard图分析对S-1·AMP-P(NH)P与肌动蛋白的结合进行的详细研究表明，在饱和状态下，每摩尔肌动蛋白单体结合1摩尔S-1·AMP-P(NH)P。随着S-1·AMP-P(NH)P沿肌动蛋白丝结合，似乎不存在协同性，可能的例外是当肌动蛋白丝上的大多数位点饱和时存在轻微的正协同性。三元复合物的浊度与单独的肌动蛋白·S-1的浊度相同。对肌球蛋白双头亚片段重酶解肌球蛋白（HMM）的初步实验表明，HMM·[AMP-P(NH)P]₂与肌动蛋白的结合强度仅约为S-1·AMP-P(NH)P与肌动蛋白结合强度的两倍，这表明第二个头部对结合自由能的贡献非常小。