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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Myoglobin content in human skeletal muscle and myocardium: relation to fibre size and oxidative capacity.

Myoglobin, muscle fibre diameter, and citrate synthase activity were measured in leg muscle of untrained and trained men and in the myocardium from the apex of the left ventricle and from papillary muscle in patients subjected to open heart surgery. The citrate synthase (CS) activity was 60% higher in trained than in untrained skeletal muscle. In the myocardium it was around four times greater than in untrained skeletal muscle but there was no difference between the apex of the left ventricle and papillary muscle. The fibre diameter varied almost threefold between the different groups of muscles with the largest diameter in untrained skeletal muscle and the with the largest diameter in untrained skeletal muscle and the smallest in papillary muscle. The myoglobin content in trained skeletal muscle did not differ from that of untrained muscle. In the left ventricle it was only 40% of that found in untrained muscle while papillary muscle had almost twice as high a myoglobin content as did the left ventricle. The ratio between myoglobin and fibre diameter, however, was of similar magnitude in skeletal muscle and the left ventricle while it was twice as high in papillary muscle as in the other muscles. In conclusion, the diffusion distance in terms of fibre diameter decreased with increased oxidative capacity (CS activity), when comparing the statistical means of the four different groups. The capacity for oxygen diffusion in relation to oxygen demand measured as the ratio of myoglobin to fibre diameter appeared to be of similar magnitude in skeletal muscle and left ventricle but was higher in papillary muscle.[1]


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