嵌入剂释放的p67的纯化，p67是一种与c-fos血清反应元件特异性相互作用的多肽。

Schröter H, Shaw P E, Nordheim A

Zentrum für Molekulare Biologie (ZMBH), Universität Heidelberg, FRG.

Nucleic Acids Res. 1987 Dec 23;15(24):10145-58. doi: 10.1093/nar/15.24.10145.

Incubation of intact nuclei in buffers containing the DNA intercalating drug chloroquine leads to release of proteins that interact with DNA. We demonstrate here that a protein which binds to a motif within the human c-fos promoter, identified as the serum response element (SRE), is quantitatively released from HeLa nuclei, whereas nuclear factor 1 (NF 1) is not. Purification of the SRE binding protein by affinity chromatography to greater than 95% homogeneity allowed us to identify it as a polypeptide of approximately 67,000 daltons. The DNA contacts made by p67, as identified by methylation interference experiments, are indistinguishable from those of the serum response factor described previously.

将完整的细胞核置于含有DNA嵌入药物氯喹的缓冲液中温育，会导致与DNA相互作用的蛋白质释放出来。我们在此证明，一种与人类c-fos启动子内一个基序（被鉴定为血清反应元件，SRE）结合的蛋白质，可从HeLa细胞核中定量释放出来，而核因子1（NF1）则不会。通过亲和层析将SRE结合蛋白纯化至大于95%的同质性，使我们能够将其鉴定为一种分子量约为67,000道尔顿的多肽。通过甲基化干扰实验确定，p67与DNA的接触与先前描述的血清反应因子的接触并无区别。