ACTIN MICROHETEROGENEITY IN CHICK-EMBRYO FIBROBLASTS
ACTIN MICROHETEROGENEITY IN CHICK-EMBRYO FIBROBLASTS
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DOI：
10.1073/pnas.74.1.120
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发表时间：
1977-01-01
影响因子：
11.1
通讯作者：
SPUDICH, JA
中科院分区：
文献类型：
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作者：
RUBENSTEIN, PA;SPUDICH, JA
次级鸡胚成纤维细胞含有3种不同的肌动蛋白种类，α，β，和γ，以大约1：63的比例，具有相同的分子量但不同的等电点。这些组分中酸性最强的是α，在等电聚焦凝胶上与心肌和骨骼肌的主要肌动蛋白共迁移，而γ，最基本的肌动蛋白，与平滑肌肌动蛋白共迁移。3种组分具有重叠的含甲硫氨酸的胰蛋白酶肽。这3种肌动蛋白均存在于鸡胚成纤维细胞的肌动球蛋白和细胞骨架中。α-的识别通过比较鸡胚融合前和融合后成肌细胞培养物，证实肌动蛋白是来自含肌节细胞的主要肌动蛋白。在成肌细胞融合后，α-肌动蛋白增加，直到它在培养物中从次要肌动蛋白组分变为主要肌动蛋白种类。
Secondary chick embryo fibroblasts contain 3 distinct actin species, .alpha., .beta., and .gamma., in the approximate ratio 1:63, 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 .gamma., the most basic of the actins, comigrates with smooth muscle actin. The 3 components have overlapping methionine-containing tryptic peptides. All 3 actins were present in actomyosin and cytoskeleton preparations from chick embryo fibrobalsts. Identification of .alpha.-actin as the major actin from sarcomere-containing cells was 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.