Bonne C, Sautiere P, Duguet M, de Recondo A M
J Biol Chem. 1982 Mar 25;257(6):2722-5.
The rat liver single-stranded DNA binding protein, S25 and HD25, isolated by differential DNA cellulose affinity chromatography was compared to the high mobility group proteins, HMG1 and HMG2, isolated from rat liver chromatin by the technique of Goodwin et al. (Goodwin, G. H., Sanders, C., and Johns, E. W. (1973) Eur. J. Biochem. 38, 14-19). Analysis of their amino acid composition, electrophoretic mobility, and tryptic peptide map reveal the identity of the single-stranded DNA binding protein with HMG1 protein, implying that the rat liver HMG1 protein becomes able both to destabilize a double helix of DNA and to stimulate homologous DNA polymerases only when rat liver cells enter a phase of DNA synthesis, possibly after a specific modification.
通过差异DNA纤维素亲和层析分离得到的大鼠肝脏单链DNA结合蛋白S25和HD25,与采用古德温等人(古德温,G.H.,桑德斯,C.,约翰斯,E.W.(1973年)《欧洲生物化学杂志》38卷,第14 - 19页)的技术从大鼠肝脏染色质中分离得到的高迁移率族蛋白HMG1和HMG2进行了比较。对它们的氨基酸组成、电泳迁移率和胰蛋白酶肽图谱的分析揭示了单链DNA结合蛋白与HMG1蛋白的同一性,这意味着大鼠肝脏HMG1蛋白只有在大鼠肝细胞进入DNA合成阶段时,可能在经过特定修饰后,才能够使DNA双螺旋不稳定并刺激同源DNA聚合酶。