Cardiac and skeletal muscle myosin polymorphism.
Skeletal muscles, unlike cardiac tissue, express several myosin isozymes during development which differ in primary structure from adult myosin. Monoclonal antibodies have shown the presence of at least two embryonic myosins, followed by a post-hatch myosin that persists until the appearance of adult myosin in chicken pectoralis muscle. Although the two major cardiac isozymes differ in enzymatic activity, the avian skeletal myosin isozymes all share the same high level of ATPase activity found for adult pectoralis myosin. The functional basis for the extensive myosin polymorphism in skeletal muscles thus remains to be determined.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D002645:Chickens; D006321:Heart / Q000254:growth & development*; D024510:Muscle Development; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D009218:Myosins / Q000032:analysis* / Q000378:metabolism / Q000502:physiology; D011110:Polymorphism, Genetic
D000911:Antibodies, Monoclonal; D000251:Adenosine Triphosphatases; D009218:Myosins