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- W2073191509 abstract "TFIIA was extensively purified from a whole-cell transcription extract from yeast. Activity was followed throughout isolation utilizing a functional transcription assay. Transcription activity was found to copurify with polypeptides of 43 and 12.5 kDa, consistent with a previous purification that utilized a TBP/DNA gel mobility shift assay (J. Ranish and S. Hahn, J. Biol. Chem. 266, 19320-19327, 1991). The Stoke's radius of the purified protein was determined by gel filtration chromatography to be 44 A under native conditions. The solution molecular weight derived from this measurement, 110 kDa, is consistent with a heterotetrameric structure of TFIIA." @default.
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- W2073191509 title "Isolation of Yeast Transcription Factor IIA Using a Functional Transcription Assay" @default.
- W2073191509 doi "https://doi.org/10.1006/prep.1994.1079" @default.
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