Diffusivity of myoglobin in intact skeletal muscle cells.
We report a method that allows us to determine the diffusion coefficient of native myoglobin in intact and mechanically unaffected red muscle fibers. The method is based on an optical recording of intracellular diffusion of metmyoglobin, which is produced inside the cells by photooxidation of oxymyoglobin with a UV light pulse. We find a myoglobin diffusivity of 1.2 x 10(-7) cm2/s (22 degrees C), which is only 1/10th of the value measured in very dilute myoglobin solutions and 1/5th of the value obtained from measurements in solutions of myoglobin at 18 g/dl. The latter value often has been used in model calculations of oxygen transport to tissue incorporating myoglobin-facilitated oxygen diffusion. Recalculating facilitated diffusion with the value obtained by us implies that its contribution to total intracellular oxygen transport is of minor importance. Furthermore, it shows that sterical hindrance to myoglobin diffusion is dominated by the muscle-cell architecture rather than by the overall protein concentration of the muscle fiber.
Jürgens
K D
KD
Zentrum Physiologie, Medizinische Hochschule, Hanover, Germany.
Peters
T
T
Gros
G
G
D000818:Animals; D004058:Diffusion; D066298:In Vitro Techniques; D008297:Male; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000378:metabolism*; D009211:Myoglobin / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D014982:Xenopus laevis
D009124:Muscle Proteins; D009211:Myoglobin