ArticleBiophysical journal1998
ATPase and shortening rates in frog fast skeletal myofibrils by time-resolved measurements of protein-bound and free Pi.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Review
- No Difference in Myosin Kinetics and Spatial Distribution of the Lever Arm in the Left and Right Ventricles of Human Hearts.Frontiers in physiology · 2017Article
- Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.American journal of physiology. Heart and circulatory physiology · 2015Article
- The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse hearts.Biochemistry · 2014Article
- Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.The Journal of biological chemistry · 2013Article
- Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies.Pflugers Archiv : European journal of physiology · 2009Article
- Real-time measurement of pyrophosphate release kinetics.Analytical biochemistry · 2008Article
- Repriming the actomyosin crossbridge cycle.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- 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
- At physiological temperatures the ATPase rates of shortening soleus and psoas myofibrils are similar.Biophysical journal · 2003Article
- Characterization of the cross-bridge force-generating step using inorganic phosphate and BDM in myofibrils from rabbit skeletal muscles.The Journal of physiology · 2002Article
- Optical determination of glutamine using a genetically engineered protein.Analytical biochemistry · 2001Article
- Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.Biophysical journal · 2001Article
- The effect of inorganic phosphate on force generation in single myofibrils from rabbit skeletal muscle.Biophysical journal · 2000Article
- Measurement of nucleotide exchange rate constants in single rabbit soleus myofibrils during shortening and lengthening using a fluorescent ATP analog.Biophysical journal · 2000Article
- Modulation by substrate concentration of maximal shortening velocity and isometric force in single myofibrils from frog and rabbit fast skeletal muscle.The Journal of physiology · 1999Article
- A weakly coupled version of the Huxley crossbridge model can simulate energetics of amphibian and mammalian skeletal muscle.Journal of muscle research and cell motility · 1999Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Shortening and ATPase rates were measured in Ca2+-activated myofibrils from frog fast muscles in unloaded conditions at 4 degrees C. ATPase rates were determined using the phosphate-binding protein method (free phosphate) and quench flow (total phosphate). Shortening rates at near zero load (V0) were estimated by quenching reaction mixtures 50 ms to 10 s old at pH 3.5 and measuring sarcomere lengths under the optical microscope. As with the rabbit psoas myofibrils (C. Lionne, F. Travers, and T. Barman, 1996, Biophys. J. 70:887-895), the ATPase progress curves had three phases: a transient Pi burst, a fast linear phase (kF), and a deceleration to a slow phase (kS). Evidence is given that kF is the ATPase rate of shortening myofibrils. V0 is in good agreement with mechanical measurements in myofibrils and fibers. Under the same conditions and at saturation in ATP, V0 and kF are 2.4 microm half-sarcomere(-1) s(-1) and 4.6 s(-1), and their Km values are 33 and 200 microM, respectively. These parameters are higher than found with rabbit psoas myofibrils. The myofibrillar kF is higher than the fiber ATPase rates obtained previously in frog fast muscles but considerably lower than obtained in skinned fibers by the phosphate-binding protein method (Z. H. He, R. K. Chillingworth, M. Brune, J. E. T. Corrie, D. R. Trentham, M. R. Webb, and M. R. Ferenczi, 1997, J. Physiol. 50:125-148). We show that, with frog as with rabbit myofibrillar ATPase, phosphate release is the rate-limiting step.
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