Relationship between myoglobin and succinate dehydrogenase in mouse soleus and plantaris muscle fibres.
This report describes a quantitative histochemical study of myoglobin in skeletal muscle fibres. The muscle fibres were classified as fast or slow on the basis of their quantitative myofibrillar ATPase histochemistry. A large range of myoglobin absorbance values was found among fast skeletal muscle fibres. This range was relatively small among slow fibres. The concentrations of myoglobin and the activities of succinate dehydrogenase in individual muscle fibres in serial sections are weakly correlated in both the mouse soleus and plantaris muscle. The myoglobin concentration is higher in fast and slow oxidative soleus muscle fibres and the succinate dehydrogenase activity in these fibres is lower than in oxidative plantaris muscle fibres in the same range of cross-sectional area.
Van der Laarse
W J
WJ
Maslam
S
S
Diegenbach
P C
PC
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D006651:Histocytochemistry; D051379:Mice; D009132:Muscles / Q000201:enzymology*; D009210:Myofibrils / Q000201:enzymology; D009211:Myoglobin / Q000378:metabolism*; D013385:Succinate Dehydrogenase / Q000378:metabolism*
D009211:Myoglobin; D013385:Succinate Dehydrogenase; D000251:Adenosine Triphosphatases