Contractile protein isozymes in muscle development: identification of an embryonic form of myosin heavy chain.
The nature of the myosin heavy chain in embryonic muscle tissue, cultured muscle cells, and several adult muscles was investigated. After denaturation with sodium dodecyl sulfate, purified rat myosins were subjected to partial proteolytic cleavage or immunological analysis using microcomplement fixation. Three types of myosin heavy chains could be demonstrated by both approaches. Whereas adult muscles contain fast- or slow-type myosin heavy chains, embryonic tissue and cultured muscle cells harbor a distinct embryonic form. The existence of this distinct form further characterizes the isozymic transitions of contractile proteins during muscle development.
D000375:Aging; D000818:Animals; D002478:Cells, Cultured; D003168:Complement Fixation Tests; D005260:Female; D005333:Fetus; D007527:Isoenzymes / Q000032:analysis*; D024510:Muscle Development; D009132:Muscles / Q000201:enzymology; D009218:Myosins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D011247:Pregnancy; D051381:Rats
D007527:Isoenzymes; D010446:Peptide Fragments; D009218:Myosins