Kobayashi R, Itoh H, Tashima Y
Eur J Biochem. 1983 Jul 1;133(3):607-11. doi: 10.1111/j.1432-1033.1983.tb07505.x.
Heterogeneity of alpha-actinins from rabbit skeletal muscles was studied. Polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate has made it possible to distinguish two closely related alpha-actinins from rabbit fast, white muscle. One isoprotein (designated type I alpha-actinin) appears to be preferentially located in the psoas muscle, while the other (designated type II alpha-actinin) appears to be preferentially located in the longissimus dorsi muscle. Electrophoretic analyses have further shown that the two isoproteins are present as mixtures in most rabbit white, fast-twitch muscles. A standard polyacrylamide gel--sodium dodecyl sulfate/polyacrylamide gel sequential electrophoretic procedure was developed to resolve the different alpha-actinin dimers and to determine their subunit compositions. By this technique, both type I and type II alpha-actinins appeared to be homodimers. No heterodimeric species of alpha-actinin were detected. alpha-Actinin of red, slow-twitch muscles was similar to type II alpha-actinin of fast, white muscle on one-dimensional and two dimensional gels. However, slow, red muscle alpha-actinin was significantly different from fast, white muscle alpha-actinins in terms of one-dimensional peptide mapping and immunological cross-reactivity.
对兔骨骼肌α-辅肌动蛋白的异质性进行了研究。在有和没有十二烷基硫酸钠存在的情况下进行聚丙烯酰胺凝胶电泳，使得区分来自兔快速、白色肌肉的两种密切相关的α-辅肌动蛋白成为可能。一种同功蛋白（命名为I型α-辅肌动蛋白）似乎优先位于腰大肌中，而另一种（命名为II型α-辅肌动蛋白）似乎优先位于背最长肌中。电泳分析进一步表明，这两种同功蛋白在大多数兔白色、快速收缩肌肉中以混合物形式存在。开发了一种标准的聚丙烯酰胺凝胶——十二烷基硫酸钠/聚丙烯酰胺凝胶顺序电泳程序，以分离不同的α-辅肌动蛋白二聚体并确定其亚基组成。通过该技术，I型和II型α-辅肌动蛋白似乎都是同二聚体。未检测到α-辅肌动蛋白的异二聚体种类。在一维和二维凝胶上，红色、慢收缩肌肉的α-辅肌动蛋白与快速、白色肌肉的II型α-辅肌动蛋白相似。然而，就一维肽图谱和免疫交叉反应性而言，慢收缩、红色肌肉的α-辅肌动蛋白与快速收缩、白色肌肉的α-辅肌动蛋白有显著差异。
