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- W2364687636 abstract "We recently found that mnany RNA polymer- ase II transcription factors are modified with N-acetylglu- cosamine residues. These sugar moieties confer upon transcrip- tion factors an ability to bind the lectin wheat germ agglutinin. We have taken advantage of this interaction to devise a purification procedure for the GC-box binding transcrip- tion factor Spl. Crude nuclear extracts are first subjected to wheat germ agglutinin affinity chromatography and then subjected to sequence-specific DNA affinity chromatography. The Spl protein purified by this procedure is at least 95% pure, and the overall recovery is >80%. In addition to yielding larger quantities of Spl than conventional schemes, the new purifi- cation procedure is also simpler and more rapid. We show that wheat germ agglutinin affinity chromatography can also be used to purify the glycosylated forms of the CCAAT-binding transcription factor. Thus, wheat germ agglutinin affinity chromnatography may aid the purification of other transcrip- tion factors that bear N-acetylglucosamine residues. Further- more, the ability to separate glycosylated forms of transcription factors from their unglycosylated counterparts by wheat germ agglutinin affinity chromatography should facilitate investiga- tions into the role of N-acetylglucosamine residues in the functioning of transcription factor proteins." @default.
- W2364687636 created "2016-06-24" @default.
- W2364687636 creator A5026016675 @default.
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- W2364687636 date "2016-01-01" @default.
- W2364687636 modified "2023-09-27" @default.
- W2364687636 title "Purification and analysis of RNA polymerase II transcription factors by using wheat germ agglutinin affinity chromatography (transcription factor Spl/CCAAT-binding transcription factor/differential glycosylation/lectin binding/DNA affinity chromatography)" @default.
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- W2364687636 hasPublicationYear "2016" @default.
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