Giancotti V, Pani B, D'Andrea P, Berlingieri M T, Di Fiore P P, Fusco A, Vecchio G, Crane-Robinson C, Goodwin G H
Dipartimento di Biochimica, Biofisica e Chimica delle Macromolecole, Università di Trieste, Italy.
Basic Appl Histochem. 1987;31(3):229-38.
The histone and nonhistone nuclear proteins extracted by different methods from nuclei of normal and virus-transformed rat thyroid epithelial cells (FRTL5 cell line) were studied by polyacrylamide gel electrophoresis in acetic acid/urea and in SDS and by autoradiography. The results have shown that some of these proteins have an higher level of phosphorylation in virus-transformed than in normal cells; moreover, an higher amount of three proteins (C, D, and E), which in normal cells are not detectable at least as Coomassie staining, was found. These proteins, extractable with perchloric acid, are suggested to belong to the High Mobility Group (HMG proteins) and to play some regulatory role.
通过不同方法从正常和病毒转化的大鼠甲状腺上皮细胞（FRTL5细胞系）的细胞核中提取的组蛋白和非组蛋白核蛋白，采用乙酸/尿素和SDS聚丙烯酰胺凝胶电泳及放射自显影技术进行了研究。结果表明，其中一些蛋白质在病毒转化细胞中的磷酸化水平高于正常细胞；此外，还发现了三种蛋白质（C、D和E）在正常细胞中至少用考马斯亮蓝染色无法检测到，但在病毒转化细胞中的含量更高。这些可用高氯酸提取的蛋白质被认为属于高迁移率族（HMG蛋白）并发挥某些调节作用。
