Sreter F, Holtzer S, Gergely J, Holtzer H
J Cell Biol. 1972 Dec;55(3):586-94. doi: 10.1083/jcb.55.3.586.
Myosins from the following sources were purified by diethylaminoethyl-Sephadex chromatography: moytubes grown in vitro for 7-8 days, prepared from pectoralis muscles of 10-day old embryos, and breast and leg muscles from 16-day old embryos. The adenosine triphosphatase activities of these myosins were close to that of adult m. pectoralis myosin. The light chains of the embryonic myosins had the same mobilities in sodium dodecyl sulfate electrophoresis as those in adult pectoralis muscle myosin and were clearly distinguishable from those in myosin from tonic muscle m. latissimus dorsi anterior. The fastest light chain in embryonic muscle myosin-apparent mol wt 16,000-was present in smaller amounts than in adult myosin. The negative staining pattern of paracrystals of embryonic light meromyosin (LMM) was indistinguishable from that of adult fast muscle LMM. The significance of these results for differentiation of various muscle types has been discussed.
以下来源的肌球蛋白通过二乙氨基乙基 - 葡聚糖凝胶色谱法进行纯化：体外培养7 - 8天的肌管，取自10日龄胚胎的胸肌，以及16日龄胚胎的胸肌和腿肌。这些肌球蛋白的三磷酸腺苷酶活性与成年胸大肌肌球蛋白的活性相近。胚胎肌球蛋白的轻链在十二烷基硫酸钠电泳中的迁移率与成年胸肌肌球蛋白中的轻链相同，并且与来自紧张性肌肉背阔肌前部的肌球蛋白中的轻链明显不同。胚胎肌肉肌球蛋白中最快的轻链——表观分子量为16,000——的含量比成年肌球蛋白中的少。胚胎轻酶解肌球蛋白（LMM）副晶体的负染模式与成年快肌LMM的负染模式无法区分。已经讨论了这些结果对于各种肌肉类型分化的意义。
