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JBC, Vol. 254, Issue 13, 5569-5572, Jul, 1979
P. J. Isackson, J. L. Fishback, D. L. Bidney and G. R. Reeck
We have subjected proteins dissociated from chicken erythrocyte or calf
thymus chromatin by 0.35 M NaCl to sequential chromatography on columns
containing immobilized double-stranded DNA and single-stranded DNA. At 0.2
M NaCl, 1 mM Tris . Cl (pH 7.5), the high molecular weight, high mobility
group proteins (HMG-1, HMG-2, and HMG-E), were not retained by
double-stranded DNA columns, but were retained by single-stranded DNA
columns. Thus, in that solvent, those proteins exhibit selective affinity
for single-stranded DNA. This suggests that the functions of the high
molecular weight, high mobility group proteins might involve destabilizing
the DNA double helix by virtue of their preferential affinity for
single-stranded DNA.
Preferential affinity of high molecular weight high mobility group non-histone chromatin proteins for single-stranded DNA
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