Abstract
Polyadenylylated RNA, extracted from differentiating primary cultures of rat muscle and the myogenic cell line L8, directs the synthesis of polypeptides in the wheat germ cell-free system which comigrate with myosin light chains under several electrophoretic conditions. The peptides also associate specifically with heavy myosin subunits during dissociation-reassociation treatment. Intact cells of primary skeletal muscle cultrues and of the myogenic line synthesize predominantly two ligh chains. RNA extracted from primary muscle cultures directs the synthesis of a third polypeptide in the cell-free system, similar to the third light chain found in myosin extracted from adult rat thigh muscle. Products of cell-free systems directly by RNA extracted from fibroblasts, reticulocytes, and myeloma cells did not contain detectable amounts of similar polypeptides.
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