Key result
The ATPase rate of fully activated rabbit muscle fibres increased monotonically with Mg ATP concentration, with a Vm of 1.78 s-1 per myosin head and Km of 16.6 microM.
Population
Chemically skinned rabbit psoas muscle fibres and myofibrils
Design
Preclinical
Authors
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Extends kinetic parameters for myosin ATPase in rabbit fibers; leaves open translation to human cardiac muscle energetics.
The study characterizes the kinetics of ATP hydrolysis in rabbit psoas muscle fibers and myofibrils, demonstrating a hyperbolic dependence on Mg ATP concentration.
Glyn et al. (1985) studied this question. Mg ATP concentration was evaluated on ATPase rate (Vm and Km). The ATPase rate of fully activated rabbit muscle fibres increased monotonically with Mg ATP concentration, with a Vm of 1.78 s-1 per myosin head and Km of 16.6 microM.
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