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. Author manuscript; available in PMC: 2009 Oct 6.
Published in final edited form as: J Biol Chem. 1993 Sep 5;268(25):18882–18890.

FIG. 1. Fractionation of HeLa S100 extract by heparin-Sepharose chromatography.

FIG. 1

HeLa S100 cytoplasmic extract protein, prepared as described under “Materials and Methods,” was separated from extraneous nucleic acid species by DEAE-Sephacel chromatography. The eluted protein was then dialyzed and loaded onto a heparin-Sepharose column at 50 mm NaCl. The heparin-Separose column was washed with 50 mm KCl and then developed with a linear gradient between 100 and 600 mm KCl in buffer BC. A, gel shift assay of the heparin column fractions for NF-κB. done in the presence of deoxycholate, which eliminates the H2TF1 protein. DNA complex (MHC WT probe). B, gel shift assay of the heparin column fractions for H2TF1. done in the absence of deoxycholate (MHC WT probe). The arrow indicates the complex with H2TF1 DNA-binding specificity (data not shown).