ATPase and Shortening Rates in Frog Fast Skeletal Myofibrils by Time-Resolved Measurements of Protein-Bound and Free Pi

This publication has 53 references indexed in Scilit:

• Kinetics of Nucleoside Triphosphate Cleavage and Phosphate Release Steps by Associated Rabbit Skeletal Actomyosin, Measured Using a Novel Fluorescent Probe for Phosphate
  Biochemistry, 1997
• Time resolved measurements show that phosphate release is the rate limiting step on myofibrillar ATPases
  FEBS Letters, 1995
• Direct, Real-Time Measurement of Rapid Inorganic Phosphate Release Using a Novel Fluorescent Probe and Its Application to Actomyosin Subfragment 1 ATPase
  Biochemistry, 1994
• A structural and kinetic study on myofibrils prevented from shortening by chemical cross-linking
  Biochemistry, 1993
• Early steps of the magnesium-ATPase of relaxed myofibrils. A comparison with calcium-activated myofibrils and myosin subfragment 1
  Biochemistry, 1992
• Kinetics of the Actomyosin ATPase in Muscle Fibers
  Annual Review of Physiology, 1987
• Transient kinetics of ATP hydrolysis by covalently crosslinked actomyosin complex in water and 40% ethylene glycol by the rapid flow quench method
  Biochemistry, 1985
• Energy balance studies in frog skeletal muscles shortening at one-half maximal velocity.
  The Journal of general physiology, 1984
• Single turnovers of adenosine 5'-triphosphate by myofibrils and actomyosin subfragment 1
  Biochemistry, 1981
• Ca2+ dependence of tension and ADP production in segments of chemically skinned muscle fibers
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1976