| Autor: |
Kawakami K; Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021., Scheidereit C, Roeder RG |
| Jazyk: |
angličtina |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1988 Jul; Vol. 85 (13), pp. 4700-4. |
| DOI: |
10.1073/pnas.85.13.4700 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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