Myosin from fast and slow skeletal and cardiac muscles of mammals of different size.
The ATPase activity of myosin and contraction time in extensor digitorum longus muscle, soleus muscle and cardiac muscle was compared in mammals differing in size. It was shown that the myosin ATPase activity of homologous muscles decreases and contraction time increases with increasing size of animals. The rate of tryptic digestion of myosin, the electrophoretic pattern of light chains of myosin and the effect of p-chloromercuribenzoate on ATPase activity of myosin were also studied. All these three myosin properties are very characteristic when the myosin from a fast muscle is compared with the myosin from a slow muscle of the same animal, but no relationship between these three myosin properties and ATPase activity of myosin was found, when homologous muscles of various mammals were compared.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001001:Anura; D002415:Cats; D006168:Guinea Pigs; D006321:Heart / Q000502:physiology*; D051379:Mice; D009119:Muscle Contraction; D009132:Muscles / Q000378:metabolism / Q000502:physiology; D009206:Myocardium / Q000201:enzymology; D009218:Myosins / Q000378:metabolism / Q000502:physiology*; D051381:Rats
D000251:Adenosine Triphosphatases; D009218:Myosins