Muscle myoglobin as determined by electrophoresis in thermally acclimated rat.

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Abstract
Quantitative analysis of myoglobin (Mb) was established using the sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis in order to determine the influence of thermal acclimation on Mb levels in muscles. Myoglobin was measured in the red and white parts of quadriceps, soleus, diaphragm and heart of young adult male rats (11 weeks old). It was higher in the red muscle (0.92 .+-. 0.043 mg/g fresh weight) than in the white muscle (0.08 .+-. 0.007), and similar in the red muscle and soleus (1.17 .+-. 0.117). Heart showed the highest level (1.52 .+-. 0.073) among the tissues studied. The level in diaphragm (0.74 .+-. 0.039) was intermediate between red muscle and heart. Cold acclimation (5.degree. C for 4 weeks, 11 weeks old) caused significant increases in Mb levels in white muscle (0.27 .+-. 0.031, p < 0.001), heart (1.95 .+-. 0.094, p < 0.01), and diaphragm (1.01 .+-. 0.060, p < 0.01), but not in red muscle and soleus. The rats reared in cold for many generations (20 generations at 5.degree. C, 11 weeks old) manifested significant increase in Mb levels of all tissues (p < 0.05-0.001) examined. Heat acclimation (33.degree. C for 4 weeks, 11 weeks old) did not influence Mb levels of the tissues. The above findings suggest that skeletal muscle Mb may be partly involved in an enhanced thermogenesis in cold acclimation by favouring an oxidative capacity of muscles.

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