Ostvold A C, Holtlund J, Laland S G
Eur J Biochem. 1985 Dec 16;153(3):469-75. doi: 10.1111/j.1432-1033.1985.tb09325.x.
The present work describes a perchloric-acid-soluble high-mobility-group (HMG)-like protein present in HeLa and Ehrlich ascites cells, rat and calf liver. The protein is designated P1 and has, depending on the source, a molecular mass 48-53 kDa and an amino acid composition which, like the HMG proteins, is characterized by a high content of acidic and basic residues and of proline. The protein contains about 10 mol serine/100 mol amino acid residues, is highly phosphorylated and has, in contrast to the known HMG proteins, an acidic isoelectric point of 5.0. An estimate suggests that protein P1 in HeLa interphase cells contains 25-30 residues of phosphate. Like HMG 1 and 2 it is distributed between the nucleus and the cytoplasm. In HeLa metaphase cells P1 is further modified, resulting in an increase in apparent molecular mass from 53 kDa to 56 kDa.
本研究描述了一种存在于HeLa细胞、艾氏腹水癌细胞、大鼠和小牛肝脏中的高氯酸可溶性高迁移率族(HMG)样蛋白。该蛋白被命名为P1,根据来源不同,其分子量为48 - 53 kDa,氨基酸组成与HMG蛋白相似,特点是酸性、碱性残基和脯氨酸含量高。该蛋白每100摩尔氨基酸残基中约含10摩尔丝氨酸,高度磷酸化,与已知的HMG蛋白不同,其酸性等电点为5.0。据估计,HeLa间期细胞中的P1蛋白含有25 - 30个磷酸残基。与HMG 1和2一样,它分布于细胞核和细胞质之间。在HeLa中期细胞中,P1会进一步修饰,导致表观分子量从53 kDa增加到56 kDa。