Rubenstein P A, Spudich J A
Proc Natl Acad Sci U S A. 1977 Jan;74(1):120-3. doi: 10.1073/pnas.74.1.120.
Secondary chick embryo fibroblasts contain three distinct actin species--alpha, beta, and lambda, in the approximate ratio of 1:6:3--with the same molecular weights but different isoelectric points. The most acidic of these components, alpha, comigrates on isoelectric focusing gels with the major actin of cardiac and skeletal muscle, while lambda, the most basic of the actins, comigrates with smooth muscle actin. The three components have overlapping methionine-containing tryptic peptides. All three actins are found to be present in actomyosin and cytoskeleton preparations from chick embryo fibroblasts. Identification of alpha-actin as the major actin from sarcomere-containing cells is confirmed by comparing embryonic chicken pre- and post-fusion myoblast cultures. Following myoblast fusion, the relative amount of alpha-actin increases until it changes from a minor actin component to the predominant actin species in the culture.
次级鸡胚成纤维细胞含有三种不同的肌动蛋白——α、β和λ,其比例约为1:6:3——分子量相同但等电点不同。其中酸性最强的α成分,在等电聚焦凝胶上与心肌和骨骼肌的主要肌动蛋白一起迁移,而最碱性的λ成分则与平滑肌肌动蛋白一起迁移。这三种成分具有重叠的含甲硫氨酸胰蛋白酶肽段。在鸡胚成纤维细胞的肌动球蛋白和细胞骨架制剂中都发现了这三种肌动蛋白。通过比较胚胎鸡融合前和成肌细胞融合后的成肌细胞培养物,证实了α-肌动蛋白是含肌节细胞的主要肌动蛋白。成肌细胞融合后,α-肌动蛋白的相对含量增加,直到它从培养物中的次要肌动蛋白成分变为主要的肌动蛋白种类。