Oosawa M, Shimaoka S, Funatsu T, Ishiwata S, Maruyama K
Department of Biology, Faculty of Science, Chiba University.
J Biochem. 1987 Jun;101(6):1481-3. doi: 10.1093/oxfordjournals.jbchem.a122018.
beta-Actinin is an actin-pointed end capping protein in skeletal muscle. Casella et al. have reported that a protein isolated from muscle acetone powder by procedures similar to those used for beta-actinin purification caps the barbed end of an actin filament (J. Biol. Chem. 261, 10915-10921 (1986)). We have confirmed the above results. However, it turned out that the two proteins were identical as to subunit sizes, peptide maps, and cross-reactivities with anti-beta-actinin IgG. The binding of the two proteins to opposite ends of an actin filament remains unexplained.
β-辅肌动蛋白是骨骼肌中一种位于肌动蛋白尖端的封端蛋白。卡塞拉等人报告称，通过与用于纯化β-辅肌动蛋白的方法类似的步骤从肌肉丙酮粉中分离出的一种蛋白质能够封端肌动蛋白丝的带刺末端（《生物化学杂志》261卷，10915 - 10921页（1986年））。我们已经证实了上述结果。然而，结果表明这两种蛋白质在亚基大小、肽图以及与抗β-辅肌动蛋白IgG的交叉反应性方面是相同的。这两种蛋白质与肌动蛋白丝相对末端的结合情况仍无法解释。
