ArticleBiophysical journal2003
At physiological temperatures the ATPase rates of shortening soleus and psoas myofibrils are similar.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 24 citations in OpenAlex.
- Training in hot water immersion improved exercise performance in hot and humid conditions in recreational athletes - a randomized controlled trial.European journal of applied physiology · 2026Trial
- Isometric slow- and fast-contracting skeletal muscle fibres have more similar cellular and molecular properties at 37°C than at 25°C in older adults.The Journal of physiology · 2026Article
- Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.The Journal of general physiology · 2022Article
- Comparative analysis of the transcriptomes of EDL, psoas, and soleus muscles from mice.BMC genomics · 2020Article
- Piperine's mitigation of obesity and diabetes can be explained by its up-regulation of the metabolic rate of resting muscle.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Effect of N-Terminal Extension of Cardiac Troponin I on the Ca(2+) Regulation of ATP Binding and ADP Dissociation of Myosin II in Native Cardiac Myofibrils.Biochemistry · 2016Article
- Chronic clenbuterol treatment compromises force production without directly altering skeletal muscle contractile machinery.The Journal of physiology · 2015Article
- The myosin inhibitor blebbistatin stabilizes the super-relaxed state in skeletal muscle.Biophysical journal · 2014Article
- Running versus strength-based warm-up: acute effects on isometric knee extension function.European journal of applied physiology · 2009Article
- Does phosphate release limit the ATPases of soleus myofibrils? Evidence that (A)M. ADP.Pi states predominate on the cross-bridge cycle.Journal of muscle research and cell motility · 2004Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
We obtained the temperature dependences of the adenosine triphosphatase (ATPase) activities (calcium-activated and relaxed) of myofibrils from a slow muscle, which we compared with those from a fast muscle. We chose rabbit soleus and psoas because their myosin heavy chains are almost pure: isoforms I and IIX, respectively. The Arrhenius plots of the ATPases are linear (4-35 degrees C) with energies of activation for soleus myofibrils 155 kJ mol(-1) (activated) and 78 kJ mol(-1) (relaxed). With psoas myofibrils, the energies of activation were 71 kJ mol(-1) (activated) and 60 kJ mol(-1) (relaxed). When extrapolated to 42 degrees C the ATPase rates of the two types of myofibril were identical: 50 s(-1) (activated) and 0.23 s(-1) (relaxed). Whereas with psoas myofibrils the K(m) for adenosine triphosphate (activated ATPase) is relatively insensitive to temperature, that for soleus myofibrils increased from 0.3 microM at 4 degrees C to 66.5 microM at 35 degrees C. Our results illustrate the importance of temperature when comparing the mechanochemical coupling in different types of muscle. We discuss the problem of how to reconcile the similarity of the myofibrillar ATPase rates at physiological temperatures with their different mechanical properties.
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