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Purification methods for the sequence-specific DNA-binding protein nuclear factor I (NFI)--generation of protein sequence information.

I Gander·R Foeckler·L Rogge·M Meisterernst·R Schneider·R Mertz·F Lottspeich·E L Winnacker
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Abstract

The paper describes a potent purification method, preparative gel retention, for the purification of sequence-specific DNA-binding proteins. This procedure exploits the sequence-specific DNA-binding affinity of such proteins for their enrichment, comparable to recognition site DNA affinity chromatography. The method was employed to obtain a pure preparation of nuclear factor I (NFI) from porcine liver from which sequences of partial peptides could be obtained. Oligonucleotide probes derived from these amino-acid sequences were used to identify genomic and cDNA clones of NFI.

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Amino Acid SequenceAnimalsBase SequenceCCAAT-Enhancer-Binding ProteinsCell NucleusChromatography, AffinityChromatography, DEAE-CelluloseChromatography, GelChromatography, High Pressure LiquidDNADNA-Binding ProteinsElectrophoresis, Polyacrylamide GelLiverMacromolecular SubstancesMolecular Sequence DataMolecular WeightNFI Transcription FactorsNuclear ProteinsOligonucleotide ProbesSwineTranscription FactorsY-Box-Binding Protein 1Journal ArticleResearch Support, Non-U.S. Gov't

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I Gander, R Foeckler, L Rogge, M Meisterernst, R Schneider, R Mertz, F Lottspeich, E L Winnacker. 1988-12-20. Purification methods for the sequence-specific DNA-binding protein nuclear factor I (NFI)--generation of protein sequence information.. https://doi.org/10.1016/0167-4781(88)90114-5

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