Lewis W G, Smillie L B
J Biol Chem. 1980 Jul 25;255(14):6854-9.
The amino acid sequence of rabbit cardiac tropomyosin has been investigated by the isolation of peptides derives from cyanogen bromide and proteolytic degradations. Based on identical amino acid compositions, electrophoretic mobilities, and in some cases, NH2-terminal analyses, all peptides were shown to be the same as peptides in the amino acid sequence of rabbit skeletal alpha-tropomyosin. The apparent heterogeneity of the cardiac protein previously observed on alkaline-urea polyacrylamide electrophoresis gels is attributable to a phosphorylated species. We conclude that the primary structures of the cardiac and skeletal alpha component are identical. Differences in actin-linked calcium regulation in skeletal and cardiac muscle must reside largely in the troponin components.
通过分离溴化氰衍生肽和蛋白水解降解产物，对兔心肌原肌球蛋白的氨基酸序列进行了研究。基于相同的氨基酸组成、电泳迁移率，以及在某些情况下的氨基末端分析，所有肽均显示与兔骨骼肌α-原肌球蛋白氨基酸序列中的肽相同。先前在碱性尿素聚丙烯酰胺电泳凝胶上观察到的心肌蛋白明显异质性归因于一种磷酸化形式。我们得出结论，心肌和骨骼肌α成分的一级结构是相同的。骨骼肌和心肌中肌动蛋白相关钙调节的差异必定主要存在于肌钙蛋白成分中。
