scholarly journals Dependence of adenosine triphosphatase activity of rabbit psoas muscle fibres and myofibrils on substrate concentration.

1985 ◽  
Vol 365 (1) ◽  
pp. 259-276 ◽  
Author(s):  
H Glyn ◽  
J Sleep
Keyword(s):  
Substrate Concentration ◽  
Adenosine Triphosphatase ◽  
Psoas Muscle ◽  
Muscle Fibres ◽  
Rabbit Psoas ◽  
Adenosine Triphosphatase Activity

scholarly journals Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres.

1992 ◽  
Vol 451 (1) ◽  
pp. 247-278 ◽  
Author(s):  
J A Dantzig ◽  
Y E Goldman ◽  
N C Millar ◽  
J Lacktis ◽  
E Homsher
Keyword(s):  
Psoas Muscle ◽  
Muscle Fibres ◽  
Rabbit Psoas ◽  
Cross Bridge ◽  
The Cross

scholarly journals The Length of Cooperative Units on the Thin Filament in Rabbit Psoas Muscle Fibres

2002 ◽  
Vol 87 (6) ◽  
pp. 691-697 ◽  
Author(s):  
Wei Ding ◽  
Hideaki Fujita ◽  
Masataka Kawai
Keyword(s):  
Thin Filament ◽  
Psoas Muscle ◽  
Muscle Fibres ◽  
Rabbit Psoas ◽  
Cooperative Units

The Effects of Substrate Concentration on the Mg-Adenosine Triphosphatase Activity of Myosin

1975 ◽  
Vol 53 (12) ◽  
pp. 1282-1287 ◽  
Author(s):  
T. Nihei ◽  
C. A. Filipenko
Keyword(s):  
Steady State ◽  
Substrate Concentration ◽  
Active Sites ◽  
Adenosine Triphosphatase ◽  
Kinetic Studies ◽  
Heavy Meromyosin ◽  
Adenosine Triphosphatase Activity ◽  
Steady State Rate ◽  
State Rate ◽  
Substrate Concentrations

Using myosin, heavy meromyosin, and subfragment-1 the steady state rate of Mg-modified adenosine triphosphatase (Mg-ATPase) was determined over a range of substrate concentrations between 10−8 M and 5 × 10−3 M, at 0.5 M and 0.05 M KCl (pH 7.4 at 20 °C). At the substrate concentrations below 10−5 M, myosin Mg-ATPase was observed to show that two active sites interact, as suggested by the analysis of transient kinetic studies (Walz, F. G., Jr.: J. Theor. Biol. 41, 357–373 (1973)). The increase in the activity at Mg-ATP concentrations higher than 10−4 M corresponds to the binding of Mg-ATP to myosin sites not responsible for the catalytic action. With heavy meromyosin and subfragment-1, the activity was best expressed by the Michaelis equation. With heavy meromyosin, the activation at high ATP concentrations is detectable, though not as pronounced as with myosin, but not with subfragment-1.

scholarly journals Effect of active shortening on the rate of ATP utilisation by rabbit psoas muscle fibres

2001 ◽  
Vol 531 (3) ◽  
pp. 781-791 ◽  
Author(s):  
Y.‐B. Sun ◽  
K. Hilber ◽  
M. Irving
Keyword(s):  
Psoas Muscle ◽  
Muscle Fibres ◽  
Rabbit Psoas
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