Talbot K, MacLeod A R
J Mol Biol. 1983 Feb 15;164(1):159-74. doi: 10.1016/0022-2836(83)90091-8.
The cytoskeletal extracts of cultured human fibroblasts were found to contain at least four distinct polypeptides, each of which demonstrated the resistance to denaturation and the acidic isoelectric point characteristic of tropomyosin. One of these, hscp 36 (heat-stable cytoskeletal protein having an apparent molecular weight of 36,000), cross-reacted efficiently with an antiserum to chicken skeletal muscle tropomyosin. Furthermore, the messenger RNA coding for hscp 36 was selected by a chicken complementary DNA clone containing a tropomyosin sequence. The abundance of mRNA coding for hscp 36 was found to be similar in both normal and simian virus 40 (SV40) transformed human fibroblasts. The apparent molecular weight of hscp 36 is different from non-muscle tropomyosins previously isolated from human sources, which show the apparent molecular weight of 30,000 normally associated with non-muscle tropomyosin. This, together with the complexity of the heat-stable cytoskeletal proteins present in human fibroblasts, suggests the existence of multiple genes coding for human non-muscle tropomyosins.
研究发现，培养的人成纤维细胞的细胞骨架提取物中至少含有四种不同的多肽，每一种都表现出对变性的抗性以及原肌球蛋白特有的酸性等电点特征。其中一种名为hscp 36（表观分子量为36,000的热稳定细胞骨架蛋白），能与抗鸡骨骼肌原肌球蛋白的抗血清有效交叉反应。此外，编码hscp 36的信使核糖核酸是由一个含有原肌球蛋白序列的鸡互补脱氧核糖核酸克隆筛选出来的。结果发现，编码hscp 36的信使核糖核酸在正常人和猿猴病毒40（SV40）转化的人成纤维细胞中的丰度相似。hscp 36的表观分子量与先前从人源分离出的非肌肉原肌球蛋白不同，后者通常显示与非肌肉原肌球蛋白相关的表观分子量为30,000。这一点，再加上人成纤维细胞中存在的热稳定细胞骨架蛋白的复杂性，表明存在多个编码人非肌肉原肌球蛋白的基因。
