Effect of temperature on the myoglobin-facilitated transport of oxygen in skeletal muscle.
An analysis of thermal effects on the facilitative transport of oxygen in skeletal muscle fibers is presented. Steady-state mass and energy transport balances are written and solved analytically or numerically using a finite-difference procedure. It is shown that no significant spatial thermal gradients exist due to internal reactions or bulk conduction effects across a muscle fiber. At typical muscle conditions, it is predicted that increased global temperature reduces the fraction of oxygenated myoglobin, increases local oxygen concentrations, and increases the percentage of oxygen flux attributed to oxy-myoglobin. The maximum supportable oxygen consumption rate, mO2max, is defined as the highest consumption rate sustainable without developing anoxic regions at the center of the fiber. By considering only temperature sensitive effects within fibers, mO2max is found to increase slightly with temperature at low temperatures. This increase is due to thermal effects on the diffusion coefficients as opposed to effects associated with the kinetics of the myoglobin-oxygen reaction. If the simulations include the temperature effect associated with oxygen solubility in blood plasma, mO2max decreases with temperature. A sensitivity analysis was performed by varying the values of relevant parameters. The maximum consumption rate was least affected by parameters associated with the kinetic and equilibrium constants and most affected by the diffusion coefficients and the concentration of myoglobin.
Dowd
M K
MK
Iowa State University, Ames 50011.
Murali
R
R
Seagrave
R C
RC
D000818:Animals; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D009132:Muscles / Q000378:metabolism*; D009211:Myoglobin / Q000378:metabolism*; D010101:Oxygen Consumption; D013816:Thermodynamics
D009211:Myoglobin; C017595:oxymyoglobin