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Biophys J, August 2000, p. 945-961, Vol. 79, No. 2
Institute of Human Physiology, University of Pavia,
27100 Pavia, Italy; Department of Anatomy and
Physiology, University of Padova, 35131 Padova, Italy; and *National
Institute for Medical Research, London NW7 1AA, United Kingdom
Chemomechanical transduction was studied in single fibers
isolated from human skeletal muscle containing different myosin isoforms. Permeabilized fibers were activated by laser-pulse photolytic release of 1.5 mM ATP from
p3-1-(2-nitrophenyl)ethylester of ATP. The
ATP hydrolysis rate in the muscle fibers was determined with a
fluorescently labeled phosphate-binding protein. The effects of varying
load and shortening velocity during contraction were investigated. The
myosin isoform composition was determined in each fiber by sodium
dodecyl sulfate-polyacrylamide gel electrophoresis. At 12°C large
variations (three- to fourfold) were found between slow and fast (2A
and 2A-2B) fibers in their maximum shortening velocity, peak power
output, velocity at which peak power is produced, isometric ATPase
activity, and tension cost. Isometric tension was similar in all fiber
groups. The ATP consumption rate increased during shortening in
proportion to shortening velocity. At 12°C the maximum efficiency was
similar (0.21-0.27) for all fiber types and was reached at a higher
speed of shortening for the faster fibers. In all fibers, peak
efficiency increased to ~0.4 when the temperature was raised from
12°C to 20°C. The results were simulated with a kinetic scheme
describing the ATPase cycle, in which the rate constant controlling ADP
release is sensitive to the load on the muscle. The main difference
between slow and fast fibers was reproduced by increasing the rate
constant for the hydrolysis step, which was rate limiting at low loads. Simulation of the effect of increasing temperature required an increase
in the force per cross-bridge and an acceleration of the rate constants
in the reaction pathway.
Biophys J, August 2000, p. 945-961, Vol. 79, No. 2
© 2000 by the Biophysical Society 0006-3495/00/08/945/17 $2.00
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