Abstract
The analysis of DNA-protein interactions is an essential step towards elucidating molecular mechanisms for transcriptional regulation (for reviews, see [1–3]). Once a specific DNA sequence which serves as a binding site for a nuclear protein has been identified it can: (l)be correlated with the DNA sequences which mediate gene expression in vivo [4–6], (2) facilitate the construction of mutant and chimeric genes for further study [7], (3) be synthesized chemically and used to purify the factor by affinity chromatography [8], or (4) be used as a probe to identify cDNA clones of the binding protein from an expression library [9]. Factor isolation and clear functional correlations are prerequisites for unraveling the complex factor-factor interactions that ultimately control transcription.
Keywords
Total Cell Extract Klenow Enzyme Nuclear Extract Buffer Hexylene Glycol Nuclear Protein FactorPreview
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References
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