Kawakami K, Scheidereit C, Roeder R G
Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.
Proc Natl Acad Sci U S A. 1988 Jul;85(13):4700-4. doi: 10.1073/pnas.85.13.4700.
The enhancer-binding factor NF-kappa B, which is found only in cells that transcribe immunoglobulin light chain genes, has been purified from nuclear extracts of Namalwa cells (human Burkitt lymphoma cells) by sequence-specific DNA affinity chromatography. The purified NF-kappa B has been identified as a 51-kDa polypeptide by UV-crosslinking analysis. "Footprint" and methylation-interference analyses have shown that purified NF-kappa B has a binding activity specific for the kappa light chain enhancer sequence. The purified factor activated in vitro transcription of the human immunodeficiency virus type I promoter by binding to an upstream NF-kappa B-binding site.
增强子结合因子NF-κB仅在转录免疫球蛋白轻链基因的细胞中发现,已通过序列特异性DNA亲和色谱法从Namalwa细胞(人伯基特淋巴瘤细胞)的核提取物中纯化出来。通过紫外线交联分析,纯化的NF-κB已被鉴定为一种51 kDa的多肽。“足迹”和甲基化干扰分析表明,纯化的NF-κB对κ轻链增强子序列具有特异性结合活性。纯化的因子通过与上游NF-κB结合位点结合,激活了人免疫缺陷病毒I型启动子的体外转录。