Isackson P J, Reeck G R
Nucleic Acids Res. 1981 Aug 11;9(15):3779-91. doi: 10.1093/nar/9.15.3779.
Proteins extracted from chicken erythrocyte chromatin with 0.35 M NaCl were subjected to sequential chromatography on columns containing immobilized double-stranded and single-stranded DNA's. Two-dimensional electrophoresis of protein fractions revealed that HMG-14 and HMG-17 are among the proteins that are retained by the single-stranded DNA column in 0.2 M NaCl/l mM Tris-Cl (pH 7.5) after having failed to be retained by the double-stranded column under the same conditions. That suggests that those two proteins possess preferential affinity for single-stranded DNA. Further evidence for that was provided by chromatography of purified HMG-14 and of purified HMG-17 on single-stranded and double-stranded DNA columns. We discuss the possible relevance of our results to suggested functions of HMG-14 and HMG-17.
用0.35M氯化钠从鸡红细胞染色质中提取的蛋白质,先后在装有固定化双链和单链DNA的柱上进行层析。蛋白质组分的双向电泳显示,在相同条件下未能被双链柱保留的蛋白质中,HMG - 14和HMG - 17可被单链DNA柱在0.2M氯化钠/1mM Tris - Cl(pH 7.5)中保留。这表明这两种蛋白质对单链DNA具有优先亲和力。纯化的HMG - 14和纯化的HMG - 17在单链和双链DNA柱上层析提供了进一步的证据。我们讨论了我们的结果与HMG - 14和HMG - 17的假定功能可能的相关性。