A histoenzymatic study of rat intrafusal muscle fibres.
The histochemical activities of myofibrillar adenosine triphosphatase (ATPase), succinic dehydrogenase (SDH) and alpha glycerophosphate dehydrogenase (alpha-GPD) were studied in intrafusal muscle fibres of rat fast and slow muscles. The ATPase reaction was carried out after the three standard acid preincubations. The cold K2-EDTA preincubated ATPase reaction product was similar to that seen following the regular or alkali-preincubated ATPase reaction, except that the intermediate bag fibres exhibited much higher activity after cold K2-EDTA preincubation. Following either acetic acid solution or cold and room temperature K2-EDTA-preincubation, followed by the ATPase reaction, chain fibres of the fast muscles vastus lateralis and extensor digitorum longus exhibited a very low amount of reaction product as compared with those of the slow soleus. Veronal acetate and K2-EDTA preincubations (and equally preincubation in acetic acid solution) resulted in acid stable ATPase activity along the entire length of the typical bag fibres but only in the polar regions of the intermediate bag fibres. On the basis of differing alpha-GPD reaction, two sub populations of nuclear chain fibres were discovered in one spindle. It is a matter of conjecture, to what extent the histochemical differences of intrafusal fibres from fast and slow muscles reflects functional distinctions in the response to stretch of muscle spindles from fast and slow muscles.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D004492:Edetic Acid; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism*; D006651:Histocytochemistry; D009132:Muscles / Q000201:enzymology*; D011188:Potassium; D051381:Rats; D013048:Specimen Handling / Q000379:methods; D013385:Succinate Dehydrogenase / Q000378:metabolism*
D004492:Edetic Acid; D005993:Glycerolphosphate Dehydrogenase; D013385:Succinate Dehydrogenase; D000251:Adenosine Triphosphatases; D011188:Potassium