ArticleBiophysical journal1996
Effects of MgATP and MgADP on the cross-bridge kinetics of rabbit soleus slow-twitch muscle fibers.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 40 citations in OpenAlex.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Oscillatory work and the step that generates force in single myofibrils from rabbit psoas.Pflugers Archiv : European journal of physiology · 2024Article
- The effect of gender and obesity in modulating cross-bridge function in cardiac muscle fibers.Journal of muscle research and cell motility · 2022Article
- Mechanisms of Frank-Starling law of the heart and stretch activation in striated muscles may have a common molecular origin.Journal of muscle research and cell motility · 2021Article
- Nebulin increases thin filament stiffness and force per cross-bridge in slow-twitch soleus muscle fibers.The Journal of general physiology · 2018Article
- Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Biophysical journal · 2016Article
- Frequency dependence of power and its implications for contractile function of muscle fibers from the digital flexors of horses.Physiological reports · 2014Article
- Actomyosin kinetics of pure fast and slow rat myosin isoforms studied by in vitro motility assay approach.Experimental physiology · 2012Article
- Measuring myosin cross-bridge attachment time in activated muscle fibers using stochastic vs. sinusoidal length perturbation analysis.Journal of applied physiology (Bethesda, Md. : 1985) · 2011Article
- Distribution of myosin attachment times predicted from viscoelastic mechanics of striated muscle.Journal of biomedicine & biotechnology · 2011Article
- Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.Pflugers Archiv : European journal of physiology · 2008Article
- Kinetic analysis of the slow skeletal myosin MHC-1 isoform from bovine masseter muscle.Journal of molecular biology · 2007Article
- Two-state model of acto-myosin attachment-detachment predicts C-process of sinusoidal analysis.Biophysical journal · 2007Article
- Force transients and minimum cross-bridge models in muscular contraction.Journal of muscle research and cell motility · 2007Review
- Mathematical simulation of muscle cross-bridge cycle and force-velocity relationship.Biophysical journal · 2006Article
- An exceptionally fast actomyosin reaction powers insect flight muscle.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Effect of strain on actomyosin kinetics in isometric muscle fibers.Biophysical journal · 2006Article
- Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres.The Journal of physiology · 2006Article
- Elementary steps of the cross-bridge cycle in fast-twitch fiber types from rabbit skeletal muscles.Biophysical journal · 2005Article
- Role of the N-terminal negative charges of actin in force generation and cross-bridge kinetics in reconstituted bovine cardiac muscle fibres.The Journal of physiology · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The elementary steps surrounding the nucleotide binding step in the cross-bridge cycle were investigated with sinusoidal analysis in rabbit soleus slow-twitch muscle fibers. The single-fiber preparations were activated at pCa 4.40, ionic strength 180 mM, 20 degrees C, and the effects of MgATP (S) and MgADP (D) concentrations on three exponential processes B, C, and D were studied. Our results demonstrate that all apparent (measured) rate constants increased and saturated hyperbolically as the MgATP concentration was increased. These results are consistent with the following cross-bridge scheme: [cross-bridge scheme: see text] where A = actin, M = myosin, S = MgATP, and D = MgADP. AM+S is a collision complex, and AM*S is its isomerized form. From our studies, we obtained K0 = 18 +/- 4 mM-1 (MgADP association constant, N = 7, average +/- sem), K1a = 1.2 +/- 0.3 mM-1 (MgATP association constant, N = 8 hereafter), k1b = 90 +/- 20 s-1 (rate constant of ATP isomerization), k-1b = 100 +/- 9 s-1 (rate constant of reverse isomerization), K1b = 1.0 +/- 0.2 (equilibrium constant of isomerization), k2 = 21 +/- 3 s-1 (rate constant of cross-bridge detachment), k-2 = 14.1 +/- 1.0 s-1 (rate constant of reversal of detachment), and K2 = 1.6 +/- 0.3 (equilibrium constant of detachment). K0 is 8 times and K1a is 2.2 times those in rabbit psoas, indicating that nucleotides bind to cross-bridges more tightly in soleus slow-twitch muscle fibers than in psoas fast-twitch muscle fibers. These results indicate that cross-bridges of slow-twitch fibers are more resistant to ATP depletion than those of fast-twitch fibers. The rate constants of ATP isomerization and cross-bridge detachment steps are, in general, one-tenth to one-thirtieth of those in psoas.
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