The relation between ATPASE activity and light chains of myosin in developing, adult and denervated muscles of several animals species.
Ca2+ATPase activity and light chains of myosin, fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, in developing, adult and denervated fast, slow and cardiac muscles of the rat, guinea-pig, cat, rabbit and chick were studied. It has been shown that in normal adult muscles the electrophoretic pattern of light chains of myosin reflects the myosin ATPase activity only when muscles from the same animal species are compared. In homologous muscles from adult animals differing in size, the size-dependent difference in myosin ATPase activity is not revealed in the electrophoretic pattern. Both in developing and in denervated muscle, changes in myosin ATPase activity are either connected with changes in the pattern of light chains of myosin or this pattern does not change. This relation is different in fast and slow muscles and also differs in chick and rabbit muscles. There are several possibilities of explaining the relation between ATPase activity of myosin and the pattern of light chains of myosin. The observation that myosin from the soleus muscle of 1-month-old rabbit contains light chains corresponding to both fast and slow type of myosin, indicates that the change in myosin ATPase activity during development is due to changes in the ratio between the fast and slow type of myosin.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D003720:Densitometry; D006168:Guinea Pigs; D009121:Muscle Denervation; D009132:Muscles / Q000201:enzymology* / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D013045:Species Specificity
D000251:Adenosine Triphosphatases; D009218:Myosins