Anderson P J
Biochem J. 1979 May 1;179(2):425-30. doi: 10.1042/bj1790425.
Double-labelling and peptide isolation have been used to examine the homology between the actin of IMR-90 human embryo fibroblasts and muscle actin. After separation of mixtures of [14C]carboxymethylated muscle actin and [3H]carboxymethylated proteins of IMR-90 cells of electrophoresis on sodium dodecyl sulphate-containing polyacrylamide gels, peptides were generated from the material co-migrating with actin by digestion with chymotrypsin. Peptides homologous with peptides accounting for Cys-217, Cys-256, Cys-284 and Cys-373 of muscle actin are present in this material, but no peptide homologous with a Cys-10-containing peptide was detected. From the amount of actin-derived peptides present, the actin content of IMR-90 fibroblasts was calculated to be 4.2% of the total protein of these cells.
采用双标记和肽分离技术研究了IMR - 90人胚胎成纤维细胞的肌动蛋白与肌肉肌动蛋白之间的同源性。将[¹⁴C]羧甲基化的肌肉肌动蛋白与[³H]羧甲基化的IMR - 90细胞蛋白混合物在含十二烷基硫酸钠的聚丙烯酰胺凝胶上进行电泳分离后,用胰凝乳蛋白酶消化与肌动蛋白共迁移的物质以产生肽段。该物质中存在与肌肉肌动蛋白中对应于Cys - 217、Cys - 256、Cys - 284和Cys - 373的肽段同源的肽段,但未检测到与含Cys - 10肽段同源的肽段。根据存在的肌动蛋白衍生肽段的量,计算出IMR - 90成纤维细胞中肌动蛋白含量占这些细胞总蛋白的4.2%。