Cooper E, Spaulding S W
Biochem J. 1983 Dec 1;215(3):643-9. doi: 10.1042/bj2150643.
Two-dimensional polyacrylamide-gel electrophoresis of acid extracts of thyroid and thymus tissue, and of thyroid nuclei, revealed the presence of three HClO4-soluble nuclear proteins, PS.1, PS.2 and PS.3, whose electrophoretic mobilities closely resembled those of HMG (high-mobility-group) proteins 14 and 17. PS.1 co-migrated with HMG 14 on CM-Sephadex column chromatography. Like HMG 14, PS.2 and PS.3 were phosphorylated in calf thyroid slices; 32P-labelling of PS.3 was stimulated by thyrotropin. Thyrotropin also induced a rapid increase in the labelling of A5, an HMG-14/17-like protein found in whole calf thyroid and thymus tissue, but not in thyroid nuclei.
对甲状腺和胸腺组织的酸性提取物以及甲状腺细胞核进行二维聚丙烯酰胺凝胶电泳，结果显示存在三种高氯酸可溶性核蛋白，即PS.1、PS.2和PS.3，它们的电泳迁移率与高迁移率族（HMG）蛋白14和17极为相似。在CM - 葡聚糖凝胶柱色谱上，PS.1与HMG 14共同迁移。与HMG 14一样，PS.2和PS.3在小牛甲状腺切片中被磷酸化；促甲状腺激素可刺激PS.3的32P标记。促甲状腺激素还能使A5（一种在整个小牛甲状腺和胸腺组织中发现的HMG - 14/17样蛋白，但在甲状腺细胞核中未发现）的标记迅速增加。
